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1. Successive hydrolysis of pro-enzymes most of which are glycoproteins 2. ‘The factors are mostly serine endopeptidases attacking Arg-X bonds 3. Bach step diminishes the effect of the preceding step causing the cascade to eventually grind to a halt 4. There are large amounts of the initial factors but trace amounts of the final ‘substrate 5. Prothrombin and fibrinogen are both found on the final common pathway ‘The following statements are true: 6 ‘Contact of clotting factors with an abnormal siirface Js a major triggering eventin: ‘the extrinsic coagulation pathway 5 zi ‘Exposure of clotting factors to tissue lipoprotein is a inajor triggering event in| extrinsic coagulation pathway B. The final common pathway of the coagulation cascade starts at factor 9, Damaged vascular endotheliuim, subendothelial collagen and glass all: ‘abnormal surfaces for the coagulation cascade 10. The extrinsic coagulation pathway is faster than the intrinsic pathway ‘The fibrin monomers: 11.Are fibrinogen molecules devold of fbrinopeptides Aand 12 Are relatively more negatively charged than fibrinogen 13.Polymertze in a quarter Staggered array to form fibrin bers 14 Are each made up of six polypeptide chains 15. Represent 17% af the original fibrinogen molecules Dicoumarol: 16.ts.a structural analogue of vitamin R 17. lsan antagonist to wftamgn K 18. Can be used as an effective rat potion 19. When injected into humans causes thé production of protronnttn wieh @ BIBBEE carboxylation of the rst 10 ghitamnste residues in prothrombit owing statements are true; co-operatively to myoglobin ai haemoglobin (HbR) has the sari 143} in foetal haemoglobin iss "2 PCH 1 Position 143y in foetal haemoglobin is histidine ¢5. Position 143() in adult hatmoglobin As histidine he allosteric manifestations of haemoglobin include: erative binding Of 0 97, The sigmoidal nature of the haemoglobin oxygen dissoetation curve ional changes in strweture brought about by a lowertng oft inability of a sharp increase in (COx} to effect any conformational change 1s haemoglobin 190, Changes in oxygen affinity brought abioutiay the binding of 23 BPG The oxygen dissociation curves for’ myoglobin and haemoglobin show that 191. Myoglobin is more arate th cngaen tanya. a 192. The myoglobin curve always ies to mete haemoglobin, 193, The haemoglobin curve has a sigmoid: 194. The Pso of haemoglobin is 26 torts: 195, The Pso of myoglobin is 4680 canna hae wae sine Fe 10 FE, faxiation ang mons The functions of the polypeptide: 196. prevention of 197. decreasing the i ty 198, bufferisg of H 100" 199, binding of oxveen 200, binding of 23°BPS Fa. YEBOAS Weis characterized by deficiency of Ribose zm he Phosphate pyrophospholdinase 174. Affected persons present with severe metital retardation 475. Affected persons present with renal calculi early in life Functions of Nucleotides: 176. They are involved in energy me tabolis: 172, They may serve as precursors {n the synth esis of tetrahydroblopeertp 178. They may serve as allosteric mediators 179, ‘They may serve as second messengers of Hormonal activity 186. ‘They are building blocks f nucleic acids Biological significance of the regulation of the de nove biosynthesis of nuicleatldes: 181 Activation of ATCase by ATP signals the availability of fuel far DNA: Teplication 182 Feedbac inhibition of ATCase by C P cnsures that blasynthetleprecirsaes ides are in aburidance 183 ading to inosinate ensaires that biosynthetic Interen ways moderate the relative abundance of a up” process in purine nucteotide biosynthesis balances the Consider the following about PREP; 155. DTP impairs the maturation off tional rRNA Allopurinol: 156. tkiey Suicide inhibitor of the activity of xanthne oxidase 157. Wis Metabolized tg ailoxanthine Which enhance the activity of xan Oxidase 158, Me react wi h PREP to. form a ribonucleotide Which inhibits Jmidophospharibosy! Tansferase 159, Winhibits both de Novo purine hucleotice b osynthesis and purine ney degradation 160, Cis useful in the ManaRement of bypertiricacmig ‘The following cause conformational changes In haemoglobin, 161, Carbon monoxide 162, Carbon dioxide 163, Hydrogen tons 164.2.3-BPG 165. Oxygen ‘The following are interactions that take place at the active sites \ haemoglobin: ‘166. Oxygen binds to the iron atom in haem. ) 167, Pree haem in aqueous solation binds oxygen reversibly for a very short tin 168. Free haem is rapidly oxidised to methaern 169. Méthaem still binds oxygen reversibly 170. With free-hiem, ahaen-oxygen-haem complex is formed before the fo: “The following are interactions that take place atthe active sites of haemoglobin: ae aaiaton pat adie E asthe residues surrounding the sixth cc we Esaluse the formation of hacm-oxygen-hacrs complexes *Yotdlnation paint prevent oxidation of the la PRINCE area of haemoglobin moet er caereaton ¢ On oxYgenation for the @rgininosuceiy, © Syothetase reacty s HiePlasmic oxatéacetare 22. Ammonia Obtaineg from amino acids are dispased of a. urea f vertebrates 23. Fumarate Vituks the a Ye to the citric ace cy te 24, The main source Of ammonia for the SYathesis of urea j dehydrogenase reaction 25. Works optimally oven When there is chronic iver disease In the Urea cycte: Amide phosphotihosyt transferase: 191, Its. bivalent enzyme 192, Its activity is Primarily control by Subs: i 193, exhibits sigmoidal Kinetics with its substrates 194, itis cumulatively inhibited by AMP, GMP and Imp 195. i *requttes AMP for optimération Consider the following about Salvage synthesis: 12S Hyponaunthtne is converted to IMP 197. tisthe main source of nucleotide synthesis tn the b 198, Adenine is converted to AMP bya 199, 200. 147. 148. 149. 150. esis of arthritis Consider the following in the contribution of ROS in the actioge™ 151 The Haber-Welss and Penton reactions are implicated ae 147. ATCase 148, Orotidylate 149. Dihydro-crotate dehydrogenase: 150. _Orotate phosphoribosy! transferase and orotidylate decs Blochemical basis of anti-cancer chemotherapy: Aminopterin inhibits dihydrofolate reductase competitively Fluorouracil (6 a sulcicte F of thymidylate synthase activity F-dUMP remain tightly bound to thymidylate synthase on formation F-UTP enhances the splicing of pre-mRNA to functional mRNA anti-sicldling derivatives include: Zempouncds thar decrease'the concentration C7 affinity of compounds that increase the oxve: Cyainate which enters red blood cells and oups af haemoglobin. Consider the following: 196, Initial OH attack can BeNerate free radicals th, at combine with gi alkoxyl radicals 197. Initial OH* attack can Generate free radicals that combine with 0; alkoxyl radivals 198. Initial OH* attack can Senerate free radicals that combine with 0 give A radicals 199, apes Ol attack can generate free radicals that combine with O2 t alkoxy! and peroxyl radicals capable ofabstracting H* and forming 200: Alkeoxy/l radical can fragment by B-scission torelease carbonpi: 106. acetyl Coa carboxylase 107. Lipoprotein Lipase 108, AMP activated Protein kinase 09. protein Phosphatase 110. Lear HDLs 111. Are Synthesized in blood 112. Are derived from VLDL | io. Are Major carriers oftrigiveerides 114. Featsre prominently in enterohepatic circulation MHS. Arsinvolved in reverse cholestern! transport Consider the following: ited by glucose and j two main forms, HDL2 and HDL3 form in which dietary FFA are carried to the tissues * gdepininosuceinate lyase and cltrullinaemta {4 Catbamoyl phosphate synthetase f and hyperammonaemia 45, Arginase and argininosuccinic aciduria Inborn errors of metabolism associated with branched chain amino acids: 46.Albinism 47. Intermittent branched chain ketonuria 48. Phenylketonuria 49, Maple syrup urine disease 50, Isovaterie acidaemia ‘The following enzymes require pyridoxal phosphate for their optimum sctivicy: 51, Histidine decarboxylase 52. Methionine adenosyi transferase 53, Cystathionine fi synthase 54. Transsulfurase 55, Aspartate amino transferase Consider the branched chain amin aniimo acts: 56, They are all essential amino acids 57, ‘They differ in that one is ketogenic, one (s glycogenic-and one 's both Ketogenic and rostabblized In. a manner which is analogous to f-oxidation of fatty acids +e oxidized by a dehydeogenase complex t is one carbon shorter than the parent compound ainly metabolized tt the ver branched chain acyl CoA which 60. The Phenyliketonuria a ie slight diluston of sk SECKION A: answa; RTUIS section ON.A SEPARATE scany, IARLE Super Inthe digestion, SbsOrption and metaboltsm of lipids: Biceaticy Lipase Degrades Phospholipase A>. Cholesteryi ster tra Upoproteins ser polytic enzyr Mecithin-Cholesterot Acyltranstorase: LCAT & “Transfers acetyl group Catalyzes the formation ofc 8 Lsinvolved ix TG motati 9. Facilitates the removal 1D. Activity decreases liver » Dhoxpphat holestery! ester ‘8 pectpheral tistves fy Hortione-Sensitive Triacylglycerol Lipase 1f- Is activated by Phosphokinase-A,v 2 Is inhibited by epitvephrine 13, Ieastirated by Glucagon (yeneraly catabou BS IRR MHyrontne and Cortcl vin regultion of promin 15. Dephosphoryhated when actiwe the adtenergs In the msetabolism of cholesterot 46, Acetoacetate is made froma Him th the mitoehonde 17 cholesterol is synthesized jn cytosol irene een lester via Mc [The mevalonate step fate eter: fg +28 Eniterobepatic circulation ts of scanners oe Sas 39. There ts: re-esterification 40 There is storage of unesterified The following are important roles of bile welds 1 ‘They prevent coagulation oftcholesterof in it > They render dietary TGs! They activate salivary and pancreatic tipases Li They facilitate vitamins-alssorption {5 They help in fat emulsification japorphyria cutanea tarda: 91. There is accumislation of porphyelaggens 2. Porphyrinogens in the skin are compared ‘93. The porphyrins may also react with xypen 94. Oxygen radicals can cause severe e slo 95, There is a deficiericy of pra joa ‘The term sickle cell anaemia includes: 96, Sickle cell SC disease ~ ‘97. S-Thalasaemla ‘98, Sickle cell SS genotype” 99, Genotype AS 100. Genotype AC ‘The vicious cycle ofsicklinginvolvess 101. Distortion of red cell shape by polymerized HBS 102, Blockage of small blood vessels : 103, Local hypoxaemia 104, Hypoxaemia causing more sickling 205. Haemolysis of red blood cells Concerning ait}-siclding oligopeptides: 106, They Work by dissolving formed HOSES repent 107. They are synthetic oligopeptides with se ‘terminal region of the BS chain 70 108, They aresteren-spectireiacion ibibo of 2 109, They resemble the “sticky pata sc seven 02 110. They resemble the “complementary ors ites” wh Isocyanic acid ant-sickting derivatives include’ as ‘plement of alph; ” n ee plement of alpha Sent a ea mia is usually caused by gene det ie mia ts Usually caused by gene deletion in thalassaemia is a mismatch of the rate of synthesis ; ofwand -enotypic forms of alpha thalassaemia are as follows: 146. Normal: -«1/act ier: -afow gmyoglabin does not have ‘a : heueine, valine methionine 151. The interior ©! et myoglobin conten parent 152. The interior of 153. The interior: ‘of myoglobin — a and phenylalanine. anime aspen ine arate, kat nreamate, a5?! —— postion act hele 154. Side chains of gh abundant in the Interiot 155: Residues that have oth « polar * ‘non-polar part paints inwal The oxygen 6. Is the co-ordinatt 157. is the co-ordina 159. Does not fal 159, Does 2 siso binds ‘SECTION B: ANSWER THIS SECTION ON A SEPARATE SCANNABLE SHEET ‘Consider the following about amino acid metabolism: 1. ‘Transamination reactions require blotin 2, Decarboxylation may result in physiologically active amine 3. Some decarboxylation reactions may require pyridoxal phosph 4. Oxidative deamination by glutamate dehydrogenase occurs in the rit. the liver S, inborn efrars ofamitiio acid metabolism are-only asyociated with essential ar acids ‘The following substances are formed directly by the decarboxylation of an amie acid 6, Serotonin 7. Histamine 8 Dopamine 9. GABA 10, Norepinephrine ‘The generation of ammonia In the reaction catalyzed b glutamate dehydrogenase: res the participation of NAD* or NADP. ds through a Schiff hase interme LL Res 12: Proc 13. May be reversed to consume a ced by inere 14, Ig ent 15, May be inti tect wh S28 of Mutation include on A ibintm 82 maar. Parasite infection among siclag coy ins MOV Hon exn, “a PeCtion =CRAd0132 cartier eng ¢ oe (SXOSE wherscys Ni DONTE, 123, 5 ribose whereas GONTP hoe / 124, FribOse suacy C2 and c3 of TIbOse sugay SN atoms at Go ONE C3 oF ji “S Of fibose sugar be visudlizeg y Staining With AUG io sar codon tron i « achcdeeptchagelinp atl restart codon Serena msec cece TA wt ; mak earache orn tor OF Geecten i re oF can pel TOPICS NT onaradset 42. isa. mixture of DNA Cee Used 10 NA og Sour ot BER weagenens Ra Co ero up at protein ot tere A Oe waits PE Gnbe used to identity the sot Regrnent of Wheres DNA ligases 746. Sr rchidouieisttanded DIES together 147, Sancho single srences OCG Together 148. Stich o double st Iandied ONA and o Wagie sanded Bt progetnet 149. Sten a single Sronded DNA and angie swanded aR toosthe 150. Siitchiyae the phospnediestot ‘pang A researchet quickly jreated o pamni-digeste? circulat plasms weetor with gikaline phosPhatos®: he rationaile tor SUE © treatment Was 1° 151. prevent re-circuianisation. of the digested piosmid: vec 152. Ennance me eficiensy “Fine gation feos" Ne ith an insert ONS 153. Reigate the picsmic ONA vector 154. pigest the plasmid pNawith ‘anotnet yestiction endonvcress> 155, Step ihe BamHI enzyr™ ctivity ADNA polymerase with 3° 156. ‘das nucieotide f orn 3 157. Removes mucIeoN 158. Removes nucleoli 159. is re quired for proot 160. isneeded for proofre’ To resolv two DNA frag 161. sps-PAGE 162. PAGE 163. Agarose \ elect 164. starch electrol penaturing PA‘ ainurneet 3 ar core 1 Enon ee orgerl Sm end vnstet Sets ne 7 a OY gone! a donirwoiaicintat ¢ fast £ fame {tro rome ee pe agonoonse nie Jwic 18. ctr are foun’ pater ise eens onetn If ees 5 Cnr mt Fi ily deter tne base composition of pNA DNA potymentzaon 1a, Proposes anes is tore’ De etween waren group of G2 OF? nucleotide and, prose pipe OI £cs of anot ther tide 17. praspho nese stomped Be etween hy: Cay FOUR OF ) ofa nucieatioe ond prosngte 1 Grour of CS of ar ather " eleoside 19.6 fomnedio 54 airection 19. Results in free phospnate te grouP” ats ond nydroxyl grouP at’ in \inear and civessar DIA 2o.no condensation reaction as water molecules 37° formed 71. inact nuctele acid, AT and G-C are maintained 22. 1s hy OOM) ponding 23, three and two hyn pondings exist between AT and G-C. respectively 24, The some arnount of energy is requil 0 break AT and G-C 25. Con De derupied with excessive hea! at, helicase pe ligases AUG io sar codon tron i « achcdeeptchagelinp atl restart codon Serena msec cece TA wt ; mak earache orn tor OF Geecten i re oF can pel TOPICS NT onaradset 42. isa. mixture of DNA Cee Used 10 NA og Sour ot BER weagenens Ra Co ero up at protein ot tere A Oe waits PE Gnbe used to identity the sot Regrnent of Wheres DNA ligases 746. Sr rchidouieisttanded DIES together 147, Sancho single srences OCG Together 148. Stich o double st Iandied ONA and o Wagie sanded Bt progetnet 149. Sten a single Sronded DNA and angie swanded aR toosthe 150. Siitchiyae the phospnediestot ‘pang A researchet quickly jreated o pamni-digeste? circulat plasms weetor with gikaline phosPhatos®: he rationaile tor SUE © treatment Was 1° 151. prevent re-circuianisation. of the digested piosmid: vec 152. Ennance me eficiensy “Fine gation feos" Ne ith an insert ONS 153. Reigate the picsmic ONA vector 154. pigest the plasmid pNawith ‘anotnet yestiction endonvcress> 155, Step ihe BamHI enzyr™ ctivity ADNA polymerase with 3° 156. ‘das nucieotide f orn 3 157. Removes mucIeoN 158. Removes nucleoli 159. is re quired for proot 160. isneeded for proofre’ To resolv two DNA frag 161. sps-PAGE 162. PAGE 163. Agarose \ elect 164. starch electrol penaturing PA‘ epout ine sh" ew taser 22 Cer or om i tee GOR ae ool Lethyris: ET tee canditian in enimnats inte) 32h acanaiiion i aim OY 23. s acquired wy tne ingestion SminoerOPl 2 hay acour when P rt oichaines is HoitateS yet orvios? onage™ acer 56. Is an iron chelator that oar remove ron rom prov ate neha en terete Naroxyiated colar ghagenwnieh eo" 2 mrevents col Irnibs prolyl pydroxylase tea 58. Inhiblts BONS formation oF unh hom at are = 60 ets the tormation of yahyaronnares & pees lif cooled below 24°C pidases otide CMON In Eblers- Da 61. Procollagen Is Pt oo rere may be deficiency Of Pr pe defective hydroaviation of YSN Mey contain pro art (I) GAG PFS 2 Paves’ 63. There may 64, Collagen ex 65. Patients show on of joints os in nascent collagen \resiaues ase: tion of allysiry @ hydroxylation Of SY) Lysyl hydroxy! $6, Is invalyed in the produc! §7 Requires 02.004 Pigetoglutarate for 1h its active site sides In pro-collager 68. Has at 69. Has Cur ot its active site the «amino groups of Vsyite 70. Acts on oxytose n of lysine in procollagen: J residues Ore hydroxylated at C-5 by lysvi ya before triple Helox formation jron chelators lutarate and ascorbate Hydroxylatio 71. A few lysy! 72. Takes place 73. Can be stopped bY 74, Requires cO2, a-ketog' jjPage Osteogenesis te at rosie ; 2 tor er aire We ar scnatinution oF esto "or a irre im e a cave jew t eoncagerovnitat eins send Bt cepests fie tattle elon ayy cmrina tere BB eran Seta Crna Red ch commen noe Sra oH He eee ic cael rehome ora eo Rectiras: = 2 to pre meen as Teal enonoe ottesciee Heb oF na conagera cheinimem aircine 1S ithe bones ond multiste ractores which give re to skelelel Je People arte gevt nate terre ee Copean eke als sate rp oe fa series eI HE Tens Cos ondonive PyeFOSIRGH on GCORVTENON Polrpeptice chains The following are characteristic of scurvy: 111. Viterrin © cteficiency J 12. increcsed activity of proly! hydroxylase 113. Lower meiting temperature {Im} of collagen 114. Skin andi other connective tissue lesions 119, Bleeding gums Concerning dermateparaxis: 119.1 s a genetically transmitted recessive disease of cattle 112 itis coused by increased procollagen peptidase levels 16 it presents with very fragile skin in attected cattle 112. There is retention of carboxy-terminal promepticies 120. Skin in affected cattle contains disorganized collagen 6/Page 2 PowCOHSSMSLIT4 14 98, Ttisassumed that all cholesterol are VI.PL. LDL, & HDL ‘99, Fasting plasma does not.contain c ms 100, Fi-derived LDL misclassifies, at the low end of LDL spectrum 101. Ifa oon-fasting specimen is used, the VLDL-TG value may he Inaccurate 102. A fasting plasma is a requirement 103. TG > 400. mg/dL indicates the presence of chylomicrons 104. The FE equation assumes thar chylomicrons, IDL, and Lp(a) are not significaat contributors to TC. 105. The FE equation asstinies that éhylomicrons, 1DL and Lp(a) are low in cholesterol SiPaue 32.8 intra-m Olecularly rr a 1ainly stabilize: valent crosslinks 1d by So} Asie 33. Is stabs # Srtabiized by banc: formed betwen some peplich Is sre ‘br ee by hydrogen bonds formed between hydroxyproh 35, Bridging water molecules . Has polypeptide chains with a type-f-trans MM resiciues ONS helix structure The following are characteristic of scurvy: . 36 Reduced hycroxylation Te Scent acwagen poypeptce Sere. Decreased activity of prolyl hydroxylase, 38. More hydrogen bonding within tropocoliagen molecules 39. Higher Tm of collagen 40. Less imino-acid residues in collagen sncering procollagen propeptide: th. They are Nand C- terminal adaiitional peptic: thay contain a reguiar (repeating) Sequence of amino: G The umino-terminal propeptides contain intra-chain disulfide bonds See carboxy-terminal propeptides contain intra-chain disulfide bonds The propeptides cannot be cleaved off by collagenases es with no functi acids activities of antibodies. ‘ . 194. Oxidative protein damage consequent to a free radical attack can! functioning of signal transduction 195, Oxidative provein damage consequent ‘wansport proteins and enzymes. tw a free radical attack can impart SiPoce % oh os ofhiyperhomocysteinaemia are deficiencies ofthe following: * g6.cystathinine f synthase 97. Methionine synthase 9a. Methylene tetrahydrofolate reductase g9. Methionine adenosy! transferase 90. Methiontne methyl transferase Homocystinuria may be secondary to the following: 91, Deficiency of folic acid 92. Defictency of witantin BL2 93. Administration of 6-aauridine 94. Deficiency of thraminé 95, Deficiency of ribottavin inate leads to the formation of ‘Transamination ofeysteine sulp! 96. Cystathionine 97.Vanillyi mandelic acid 90, Chenadeoxyeholate 99. p-sulfinylpyrovate 190. Normatatiephrine Consider the following: norrnallty thionine y-lgase due to detective 73: Tetrahydlrobiopterin 74. Neavety! glutamate 75.S-adenosy methionine ‘react to form polypyrryl methane react to form uroporphyrinogen | Fenet 1 Formuraporphyrinagen iit under the action inogen deanstinase iif.co-synthase tsomerises uroporphyrinogen I cs eure eon converts uroporphyrinogen II fo Coproporpiiyrinoges Ti oxido-decarboxylase 6.Acts on two propionate groups: side chains 7 0 36 Aas on pwo propionate groups side chains 6 35 Desarboxlates and then oxidises to Propion oe Reaverts coproporphyrinogen Ii t protaparphyr: 60. is inhibited by lead a4 17 ide chains ogen IX tons: sn synthesis are properly matched with thel ‘The following enzymes inh n CUPG) | synthase: condensa! en secon Be auctale, ments ree raocleil Bh ipne ‘Bhima M cmscciaters at conmn “Grant a a os sow eee eoethicd ONS Soret ot fos oe aera igen rhc” ‘Sei Wot RNA o eponmurnags 3 ae 3 ee nor, ron roar 3 un eee, ot ern ane vn ou et Jeic A ori nyenine are pound ar voile golds Anon? maior 1016 purines nove puso? rings pee nyeming thet cytosine 9 COTOGNY ‘determine ‘the bose composition of DNA DNA potymentzon 1a, Prope o Sees pana stored petween 2 droxyi GrouP ot c2ofo pucieotiee bed POS group. of C8 ‘of anotner nucientide 7. prosphonener ’ rormed paNweer hydroxy! arouP of C3019 nucleatide ond phospnate, growl of ChOF another nucleoside 10. s formed i 57-3 cretion 19. Rests in ee phospnate group ats ond pydroxy! grouP at 3’ in finest and civessar DNA 2o.no pation reaction as water molecules 37° formed acid, AT and G-C are maintained between Atand GS respectively id G- pose 2. is hyooer™ ponding nd wo hydrogen pondings exist nt of qnergy requires to break Ach an ve heat, helicase and ligases \ 23. three 74, The soe ornov 25. Con De digupted with excessve Hvpmcmosocieciton of te pesarncd tern Gaciire OF tthe-roic) ctl ie thom eeires ISS i 36. The acavisifion of GOP by transctuci Fhe aetivahion of a prospriccieostercse verter fo MP in tne rod Sell [39 A decreases in the level of Ca 140, A Gecrease In the level of CY: sterase involves the following steps Activation of rod cell phosphodie: 42. Activation of GDR-transducin by PHOTO! 14a, Acquisitian of GOP by ransaucin py. Detachment of a-ransducin-GiP trom the wilh phosphodiesterase 45. Hycrolysie of GDP to GMP bby a-transaucing \ysed rhodopsin By subUnits ancl association recovery In visual excitation involves: 146. activated rhodopsin being blocked from continuing to activate ranscucin 47, Rhodopsin kinase catatysing the phasphorylation of the amino-tenminus of activated rhodopsin at multiple serine and threonine residues 2 Aresiin, an inhibitory protein binding phosphorylated rhodopsin anc preventing 2ciditional interaction with transducin lowered intra-celiviar Ca* jeading to inhibition of quany!a te cyclase pag OHSISMS274 —16 picaars Trey respec elaen acaitional peptides oa rior arrine etic tosance to the eit at na poWwpeBtte tae. oh 185 FREY. re Hh in eyes 128 TRS omincsiaeni INS. BrOliIne nd hyaranyprolina: Propepfides contain inira-chain cisuifice DON jwuitete: bonds Sob oxy-tonrn 185. 1he peony Imiminal propop tices cartain mbachan ore cleaved by collagenases Conce; eet eining covatent cross-linking within collagen: ISS bysine ant hydroxyysine residues are involved IBZ. Proline cine myaronyporoine residues are Iv alow 188: It involees the action of ty3yl oxidase : Hvolves the action oF Iysyl HYAroXyesS 90.1 involves the conversion of Ihe s-arnine Group of lysine to an aldehyde Collagenase. 197. Is an enzyme that cleaves peptide bonds located within the characteristic helical regions of collagen 192, from clostridium histolyticum cleaves collagen at more them 200 sites 193. From human tissues cleaves collagen at more than 200: sites: 194, Action produces gelatin 198. Is involved in the remodeling of scar tissue The fellowing happen when heating a solution of tree tropecollagen molecules: 96. Large changes in 7. There is a sharp re jemperature . There is an increase in the optical helical structure of the strands. 4 There is an abrupt transition from iropecollagen to gelatiny rhe melting curve of collagen when plotted is parageolic physical properties occur at a characienstic temperature duction in the viscosity of the solution ata characteristic rotation of the solution indicating loss of tne actse ore FALSE sccimpenssetit tere ce gone Olas oot > pioore « mer anee, oo" oon ee on aceon Oa gana? 4 open tee ot tan HOS & tasers ie 7 OMA Wn eve! Ae arn One Te reere MEE Ioan einogenes b ous poses OF acids 7 pepe OI pel gu a inyrnine are found" pwcisie alt “ord CRO? prrcona. io ne ee ere Ise HOSE ig naan CYTO jatermine wh pose comp: ives sition of DNA 12 fo pucieotite 15. coven © DNA potymertzanion pe esti OOO roma DOPTeST T arenes grouP © ‘C5. of ANON! nucleotide 2 tn hy-arony! FOU of 30F pr nucleoside yl grouP at3' a nucieatide in linear and med dG-c are maintained acid, ATO” exist betwee! i eak ponding drogen bondings of energy is required to excessive heat, helicase and ligases 5 double BRING © soUble digestion of 20k DNA with Eco! Bz only 4 DNA bands conte een on ene Barntit Be GNA agra cre seen on on agar 85. PAGE can be Dre ee bbe Used 10 1 foo Oi ei bar Tits shou loka plasmid DNA DNA hos : has 2 Xhol site: 87. Onty 1 A fragment sizes of 3.5k and 500bp ore prod these plasmid ol and S005p are produc 88. 3, ¢ and Bk ae duced Ree ee Ne ee eee piesa ONA Danio the aigested ples 90. ligase fs the en x sed in procedure 117 J from the plastria 1 okt Polyacrylamide get electrophoresis (PAGE) 1 Is for separation of RNA and DNA fregmer 32 nagar 93. son excelent for enarocterng ative protein 94: Higher moleciicr weight ONA will travel faster tN Be ee inact from seaweeds canbe used to make PAGE d starch gels 2. Has a superior resolving power than cary sme $-PAGE, which showed 18 ,eparated on SD° sri lot ct from blood was 5 in. Following probing of West Juding albumit nti-albumnin, Protein extra: protein bands inc membrane with a 96 Appeorance of 1 protein band is an inciesYen blotting w 37, 15 protein bonds wil be seen on ine membrane 38. The position of the albumin will change °° the 99. Only albumin band will GPPESt 100. ‘All the 15 protein bands will be franstered onto jasrit success em blot membrans the membrane DNA. The 4 letters form lettered ‘A, G,T& C)in every ons can be formed There are 4 letters ( How many cod words called codons. 101. 24 102. 64 103. 48 104. 12 105. 128 DNA replication in bacteria 106, ofiC is not essentially required to rept aS 107. Okazaki fragments are found in both song Sl a 108. Helicase is responsible for the unwinding: f parental dovdie ik 13|Page histones bh ‘ epout nucle, ay ick ONA ST, ences ot Cece ai ae amcor ore | fame, gar at * erties Shoo 5 rears IAPS Tien eile s pases of UE! acids aa 11 AOI opowre: ino ond tt ne ares FOUN jan pucieia ate ip ngewe, ord OO? sarong 10 ne punnes 13. Tryrriow eed Fare tusee ings ja rot ig sect NY sieritcat 10 ITY! ‘ine whan cytosine 15. EON? erorgon was fest 10. corTony ‘getermine he poss composition of DNA DONA 16 sor ponds petween pydraxn atouP per oe pucieotite ne capa FO Fes of anoinet nucieotid]e 17. prosphonene pond is form petween hyarory! grovP of CZF nucleotide ond prose, grour of Ch OF ther nucleoside 18. is formed i 5-3 rer 19, Results i free phospnote grou ats ond pydroxy! group at 3’ in tinear and cirestar OA 20.nso sation reaction a water molecules are formed Gc ae maintained ny Atand GG. respeciively pose zi 22.18 hydroge”” 23. Inree ond two hydrogen bondings exist betwee! 24, The sone arnount of energy 5 required to break AT and G-C disupted withexcess¥e heat, helicase and ligases \ a Oy athe es na Seca Sonepat Toned win sorte sae are eet cn on egg elogen aciditional peptides: MII OMING ele sequence te the rest chine povpepiae ny a 183. The ete EN 9 glycine. roti cra trcromoreties 4. The Saino-totmiral propeptities Canton iivarcnean alsuiticae Darts 185. rng LMPOxy-tmeeninel propepiices sentain hives ahain alshete BONS Propeptides ore cleaved by colagenases Conce, 0 ees eining covalent cross-tinking within collagen: IBS: bysine and hydroxyiysine cericiuer are involves I8Z_ Proline cine) mrciroyproine (exiaues are twvalnet 138: It Involwes the action of tysyi onieace [2% it Involves the action of hay! hycronyiare It Involves the convertion of the «amine atoup of lysine to an cidehyss Collagenase: 197. Ip an enzyme thot cleaves peptide bonds located within the characteristic helical regions of collagen . 192. From clestriaium nistolyticum cleaves collagen ot more than 200 sites 123. From human tissues cleaves collagen at more than 200 sites 194, Action produces gelatin 196. 's involved in the remodeling of scar tissue The following happen when heating a solution of tree tropecollagen molecules: 96. Large changes in 7. There is oO sharp re\ temperature . There is an increase in the optical helical structure of the strands. There is an abrupt transition from jropocollagen to gelatine rhe melting curve of collagen when plotted is parabolic physical properties occur at a charactetistic temperature duction in the viscosity of the solution at a characteristic rotation of the solution indicating loss of tne oe UG ka start cor cc arenarcr os protein syntty A coding region ova. genotist Shiv re sex Renn coming on arson saan cue | inka it fase plays inmpartant role i" ance merase ea proran noms 9 geen Benet lade ay eg deecton ce tne tunciiensot DNAIASO- Protein marker con eavoly 121 Ket SNA agments of YONG BEE DNA taaenen® nines oe Isa mixture: —_——- Me ro quaniity the onouny he made ves ein oF differen molec weights aresale Ug ya identity ne ONS RGN nt ot eres! DNA ligases 146. Sr rchidounteisteanded DIK. together 147 Sate wo nee STEM DNAS together 148, Sich o double s¥anSSs ON nd ange HONS minragenet 149. ste B single sanded Oe A om gle srenaes aN togetnet 150. Stitch yon the phospnodiestet ‘pond treated 2 pamui-digestes ecutar plas weetar with was te er quickly A research The rationale tor such? piosrrid vector! at DNA ‘alkaline phosphates? 151; prevent re-circuiarisavion: ‘of the gigested 152. enhance Ne efficiency of fhe jigation reaction saath ON ISS" 153. Reigate the piesa DNA vector 154 Digest the piasmic SNA witty anolhyer FS* sation endonysress> 185. stop the BamHt enzyme tity A DNA polymerase with 3° 5 exonuclease activity 156. adds nucieotiae porn 3’. 5) 00 HO strand 187. Removes nucleon om tne & ot ine grand 158. Removes Mcieotice from Ine 3 of the stron 159. is required for proofre ding Bunine replication 160. js neede' for Pros reading in remses To resolve two DNA fragments ofl commended *° use 161. sps-PAGE 162. PAGE 163. Agarose gel electropnores® 164. starch siectropnoresis Denaturing PAGE 165. 138. Mew Feo cS inn 120. met ors oe peeve el tynyl rescues 9 pro=conoge” When fitroblasts are exposed to TGFD1 matrix 181. They increase synthesis of collagen and other sxlracolular poresten y matrix 182, They increase degracation of or gen and other extrac rote 183. They increase secretion of proteoses 184. They increase secretion of protease Inhitsitors 465. They may be transformed inte myoflbroblasts Concerning procollagen peptidases: 186. They cleave procollagen extracellularly 167. They ate collagenases 168. They are matrix metallo-proteases 169. Their deficiency can lead to Ehiers-Danios syndrome 170. Their deficiency is associated with increased content of procollagen in skin extracts The following contain nermal amounts of collagen: 171. Normat skin 172. Normal scar 173. Atrophic scars 174. Hypertrophic scars 178. Keloids ge PowCOH 8 double a ligestion of 20kb DNA with EcoRI and BamHI able to fhe agarere gets sek jynemeth ee aie. lasmid DNA hy DNA has 2 . as 2 Xhol sites of 3kb ies ae tance avertieare cows ment snes &% Ont 1 trace arent sans of 2.64 and S00 ore Fro ere anaes oe from the tear DNA plasmid DNA fo wil pre 90, ligase is the enzym 3 from the plasnis duce V1 5K sed in procedure 117 Polyacrylamide gel electrophoresis (PAGE) sparation of RNA and DNA fragmer power than agarose and starch gels tering ative proteins jravel faster than to make PAG 91. Is for 92. Has a superior resolving F 93. 's.an excellent for charac! 94, Higher molecular weight DNA wil 95. Juice extrac smaiier weight in PACE + from seaweeds canbe used $-PAGE, which showed 18 arated on SD: ern blot ct from blood was sep: Following probing of West Juding albumin. nti-

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