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    16 views10 pages

    ProbIemasIBQI PDF

    Uploaded by

    Peter Tate

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    © All Rights Reserved
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    of 10
    Py heat grined by Sowing mediam, calculate the maximom tere ture Fe obaicabe fora single enzyme-catalyzed reaction in term of best of reaction per mole reactant AH, fastonal conversion of eactan eactan inlet concentration fii heat pacity Cyr 896 AT'S Tass ~ Ta 10) For BD 'Prcent hydrolyse of 20% lactose rolation (4/4, = ~7100 lig tal). show that the maim temperature rise i oly afew degrees Cele, (6) When a cooing jacket is applied oa thin enzyme rector, he eit centerline temperature approximately given by where ¢= colin length = evidence time of fui, and a= pC, where fy ~ overall thermal Conductivity, p= packed bed dens, and ef i the efor function ubulated for the argument, {axa a any handbook). Show tha forthe conditions of part (Bk, T* Spproachessnity rapidly (ealeuate 7° when r= 1,2 3.4) (7) AIX. Malle immebitiedemzymes Employing the Siln-heory Mealiation, investigate what happens ‘when consecutive reactions s—~r—“ ce ‘occur in an immobiaedeneyme sytem, The enzymes E, and E, are both atached toa nonporous ‘Support surtace, the enzymes are intimately miaed and uniformly disbuted on the support and the rates ofboth reactions ean be approximated using Sirstonder kines. (a) What is the rate of disappearance of 87 How the faction of S which is converted into P Meced by the mass-transercoeficiet of R? (@) How would you expect the answer to the lst question to change asthe average distance between Ej and E, molecules scenes? ‘RIA Hyseresa: sabtrte lahiblon An enzyme which exhibits substrateshibited netics {[€s. 652] immobilized onan impermesble soll sucace. Assuming that the stagnant mode _ndeqatelydeseiBessubrtzatetassprt fom the bulk ud to the surface, determine observed dimes ones reaction rates) or each of he following sete of parameter vals and \ot 8 wk, feo ‘8 For parameter st (0 plot in one figure both the dimensiones rate of mas ans tothe surfice and the dimensionless sue reation rte vx, the surtce substrate concentration. What phy ster- etatiocan be attache tothe inesetion(s) ofthese curves? Dacuss the posible sigiicance of your reult with egrd to design and operation of ismobilaed-nzyme reactors For anexpeinental ‘emonsvation of the phenomenon you have discovered, see Rel 8 GENERAL REFERENCES Sema ‘The constant synthesis and degradation i called surnocer, The synth- “anconme trove pects The re prec “The degradon af an enna Gh folaws fsvarder Lneict "That iy be Tate of deqrad Oo othe concentration of enn pes folvng prob ss Kins ye Meh Nhustrates the relationship betwee ec acai Broly ° chance th Fee Kgl Sua Enos Bev fof Roped Ete ens Gate Enea eons Yan Se Fe rae me in Rad the So pat: gen Po cone ms mt sem 429 rmieniearmncees Ratu Cmte or = FS ctedyenate inte of UTES Wee, J. Emme Calais, Harper Row orccular enzyme of liver is synthesized ata constant rate of 12.5 . Seas Shaymes altri enzymes ot0Pe (69), nies per xchange and membrane sPO"% yefen, E and Pt, Hall Th Sal al oa tsueper minute. ‘The teadysatelevelo he en thre (a Cael the frvorde rae constant forte deqradaton ef he ne) Anan of shone wo he rate of me synthesis to increase sixfold without affecting th cfs nicer wv of degradation, Aleta he nen sted sn sce tte What is the new rate of degradation? es f degradation?” What isthe new steady-state “Gcbonims. | Wileytntericience (W973) Gover Expy itater, JR. Pritips of Eneymalog or he TeeF dienes Matcel Dekker (1972. PRACTICE PROBLEMS In order t0 maintain a TE}, af 250 units per gram tissue, the rate of Annwers 0 Practice Problems ave given on pages 420-428 ation must ‘equal the constant rate of synthesis. The concentadonrcledy ta oe a ee ould Son ang bse fe and en wen ewe tS 6 ren Soe ak ie ence. oboe bre one? Von 2, Meuron tines eaesate a pO i or cnrme |S TE cn constant ft te Be enraion emloye sion Sunes 210%, Eneyme Fat the reaction (Kq725%107M. Wine 2 et ain Ca What ee 3 * a2 ume ttr the fread _ Rote na th rarer ae cons ne Bags BEE ee 38x10" % 5. An enzyme catalyzes the “reaction his units x g tissue” X min” to maintain a new stead} sx s min, Vm, = 4 moles * titer? * wena ene ig o min”). In which direction ‘and how fast will pe = eh Ie ae eat ee he OB Soe nina nat nea Werte ar, "by 205, 27 amotelict Men had been produced. How Ssh a am comme with a K. of 410° Product be presente min Oh = : wo ame ae ie an Sy, ok Eyes (0 wha parent ncn in he ro nme we aye he EN) SEIU A Sneath wit wer” con CMe oe 8 es sani at O08 M wae velomics Am enazme wil 4 wens ancl ata nial subarate concen Meuhe ener subarate concentra ed 9 evevses fon of 03M. The obverved veloty was Soe to? moles tere mie Whe nak rere een wee 210" a ould te predict concentration be ate (a ‘bin and) 10 min? Heras 4. Anenzyme with 3 Ky of 3x10 AF was usied aan nil subase concentacion IM, By Linn, 305 of the substrate Pad een utlized. (a) What percent ofthe sub- rate wil be atid by 3 min? (Uf the ini barat concenration mere 8 1", ‘Year percent ofthe substrate wil be uti Bp 8 min? (e) Calculate Vax (@) At 8X TOM, how fong wilt ke for 50% ofthe subsrate 0 Be atlied? fe) AC IM, how Tong wil take for T5% of the substrate tobe wilaed? s ao Ler 10" 25x10" sno" 30x 10° 70x10" Lox tot Txt" 1érx to" 20% 10" 30% 10" 9. cals bh (Sh 6 isha snd [Shs fo aC Ze that obeys type stration kine 18 The fp ax of ly ans of espe plo i seat ol nin) Tae as atest 0 15 The pot tne he we eh 2" Teneanehs Wate Vor and na ‘mocghine-binding substance was Sted rom in te The mari at ered to homogzney and Wend 3 reoprotin of MW 26.90, “slain of Byeoprotein (030 gin) was dalyed (Buta for Practice Problem 12) ins an qual volume of 2 solution of Emote Ae eam, he caer containing the gicoprotein contained {A33 1O*H tral (bound + fre) "H-morphine, The chamber without the, glenprotein contained 0.78% 10° "Hemorphine, Clea (a) she conceatation of boustd " rorphine, the cmeceteation of fre peo- {eins an (6 the disocation constant for the Rheoproteinmorphine complex. ASSUME fee binding see per protein molecule 12, Embryonic liver tissue contains a en syme tt camhynathe seaction S=®. Adult TiveralsodsplayeS->P activity. Some Kinetic dita areshown below, What conclusions can you draw concerning the identity of the «wo (Oberoed nial Velocity (mala ng Protein = Min) ‘Estat of Adult iter) strat of Emirjonie Lice (E9 105 re ‘500 1.98 neal i 2 8 at 1.87 : i 1%, During severe liver damage, an en: zyme (E of practice problem 1) i released iieo the oaageam.” Aber severe exercise, a muscle enzyme, Ey thac eatalyes the same (Bata for Practice Problem 18) s v ele mle min 8 aT 8 100 1 v0 00 rection sree into the blood steeam- Tere cn be diferenited easly becuse hey tae diferent Ra values. (The Ke of herman enzyme e210" 9) Ansa rood espe of patent gave the cess Showman 320, Isthe pavent seller trom er duce; or as he simply been exerci Mecauoadh) (The patient arived ae hoF Initial Velociy (nmolesimin) (Data for Practice Protiem, ‘Siwsty (Contd) rok 6a oem eT BRB oo 20188 oss e098 1000 bso S888 SD too S000 $8.00 oT 40.00 tM BAS S33 Togk 8283 feo soo STE Soo sas 6250 50 as ee pirat conscious, 3 you can wk tm ar fusions) 1 Caleulate 1 and the degre of inhibi sion caused bya compesiive mibior ender ei toming condiions: (a) (S]=22 107 wey tnnax 0? Mf (0 (9) AEM aed fap#2 10° af ad (6) (S]=75% 107 M and signe Asume that Ky =2% 107M, Ne and Vine = 270 moles x Zioknmecrmansarts satin i required to yield 13% inhibition at ‘otibte comeenration of 15X10" M if jcanax tea and Kin 2x 107M?) JF Tat concentration must the substrate BE verre un reestabih the vlocky a the Driginal uninhibited value? 16 Caeulate K, for a noncompetitive in- bor if 2 107M (] yields 75% inition Shan eneyne-catalred rection. 17 Caeate (8 the sel and () the degree of inhibition of an enzyme craiaed SiS in the presence of 6% 10" M sub Tea Te 10M) and 2510" M none Competitive inhibitor (K, =3*107). The ae sis mmoles iter" in" TR. What isthe rlaonship between 6 suobrate concentration eequied i the pret+ raacrics @ROMLEMS. 221 ence of 3 compesive inibitor, SL to the ‘SUoneme concentration required in the ab- ence of iohbitor (Sh in order to observe a ven veloc? 1a, The folowing velocity data were ob- tained, Determine the nature of each ia- hibitor and calculate Ke », TeawomM TYadmM +Zac02mh 338 10.90 6a nt a3 23) nt 12 6s 1660 ne 188 Bal 1832 eH (a 2557 19.0 nat 1923 4h. ‘The produst of Uni Uni reaction, achasa compernsenbiiae with Fxpett 0S Teen? and Scommpete for free EW Ka 8 Ce age (Vou, very seal Be equstion tor the forvard ee i -—_— = (ery Consider a system where the tot pool of fhe iPlis conta and equal 010" M. Ks Tee Kee WM | Vag = 10 mmoles Tree cmint What wi ee =) versus (S] Behe look tke? Keep ia mind that (SI WM, (2), ret? m Thus, at) = Sreaoe ate at (S}=2e 10" Me (RBH 1O M, and 50 of > th The sate ofan ene is he A 43). The active okt ereyme contains a hstiine reside (hice ds) aha must be protonated for actt~ (eeu What isthe BF optimum of = ‘p, -The active ste of am esterase contig an yeiaie, aed a baie amino acid Substrate binding occurs only when TANE-COO™ Thus, he Ihe Sine species is “HNCES-COO™ while BReygN ES-COOH and N-ES-000" species sop ents do noc exist: The p's ofthe two eesidues Je 40 (PK) and 7.0 (pK), (2) What i che 3 optimum? by Write velocity equate Ffprving the effet of [1°] on 2 21 and 37°C wat 140 amoledy 78 Vn especialy. Caleshte (a) the ateation feergy and () he Qu value Hetween 28 nd sc 24 A cclitrce extract of Buchrichin colt conmsins “Hing protein per miter. ‘Teenth microlers Of thi extroct in a stan dard incubation volume of Ot cxayeed thetacorporaton of lucore"C fom ghcose- phsephate-"© into glycogen at a rate of Ubnimolemin. Calculate the veloc of the reaction in terms of (a) wmolesinin, dnoleslte"emia", fe) gmoles «mg rote min". Alo ealeulate the phos: horas atv ofthe exrsein terme ot 18) Soil and fo) uniwing protein. 2. Fey milters of the cell-free extract esetibed above war fractionated by 20 ‘onium sulfate precipitation. The fraction precipitating between 30 and 50% siuraton nt redisiaved in a toa volute of 10 il and Giabaed. The ‘olution after diye oe fayied Wem and conned eg, protein, Twenty aicroliers of the Poti fraction extalyred the phosphorylase Fescion ata eat of 59nmole/min under the seandacd seiny conditions Calle (8) the recovery ofthe enayie and () the degree of punfeation obtained in the ammonaam sl fe step. 16. Apuseennyme bara sgecfeatvieyof InVunising protein. (a) Gaculate ue cam oer number if MW = 360,000) Calculate the tie requited for one catalytic yee 1. a) How many ite of hekinage ‘ust be added 9 Ul of reaction volume 19 vse up 95% of Bc10°M glucore in Bain? KeAT IDM, ) How long oul take Lenker owe up hese oun of glucose? 28. Caleulte the delociy of an enzyme. ‘aulyaed seacton ASB-*P+Q 9 (A]= U5 “snd (Bl 67107, Assume "fat A and Badd randomly tothe ensyme and (aha ~The binding of one substrate has no exon the binding of the her, (0) =O. lhe binding of one substate decreases the sociation constant forthe other by 3 factor (Of 10). Proliminaty experiments etablshed that Ky222 10" My Ky 1910 M, and Te atmo erm fe Yuet in" and #00 ames iter" mid “teady wate ordeved birearat ster to show } 29. Reasrange the velociy equation for 1Van a8 (a) {A} is varied at diferent fixed Concentrations of B and (@) [3] ix varied = diferent Bxed coneentestions of 3 50, How do the reciproeal plot fora rapid qulrium ordered byreactat system ifr fro thor of 9 steady-sane ordered bites tan system? 3H. What ecatve values of ab, and ¢ Gaverction. tore) would eld a ¥elocsy ‘urve foran allosteric recramer that exited postive negative positive cooperativity? 32, ‘The following data were obtained for an eaymecstalveed eseion. Determine Shether the enzyme obeys hyperbolic oF mmoidal kinetics and calculate or estimate the appropriate Kinesc constants (K, and Van, OF Ks Sho tay ad Vn tal Subrate iia Concentra Welty Gag) 635 1s 350 509 1009 2000 smn se B61 (els Xie min) 3%. a) Whats he ow alue of a enryne [Spuisje 89? 0) Caleulate the (ShulSh ratio ofan allosteric enayne where Maw = 34, What isthe vale of L fora allowerie Aimer (2) Ho) Vag 93S when (SVE SF Awume c=, 35, The concerted-symmetry model does rot forbid T = R transitions among paral filed’ complexes. Tf La defined au (TSVERS}, and Ly i defined 36 (TSRSY, that ae the values of Ly and Lin terms of ard o Consul Fig. 433, 6, “The level of 2 pariealar smeyne & st unnig thse in the iver of 8 08 a atu diet.” Studie indies that the fr BRher rate constant forthe degeadaton ofthe Sayee 8 OOS rin) Caelte he seo, Srder rate of enayme synthesis (8) Whe are raised on a completely she det the ateadysace level of the above ensyine f decease o aS unig tinue, fhe rate o hone shes uratfected Dy ict. what Grae the new fisvorder rate comtant fot PRACTICE PROBLEMS 323 enzyme degradation be?_ (6) Ifthe firsvorder frie constant ob ensvine Gegeataion i uo ‘Bete by dit (nd femains 009 min”) what must the new reroorder rae of enzyme Synthesis bein order to mainin (ED a the few evel of S48 nts tissue? [Also s0e the pastice problems on enzyme sea it the chapaers an "SpectrophioworetTY Sed Other Optical Medhods™ and "uotopesin Bioeherisy.”| 496 aNswers Tro pRacTice PRoMLEsIS 28. AH = -70.00Dcalmnle AG" = 65314 calmole, TS =~ 856 calimile, AS = 15 eu at 35°C 08K) 2G) aH =—c10m catimole, 36° CHAPTER 4 ENZYMES 1G) Ryn 10M, Vow = 129% 10" MY nin (bt Very by pling versus ing 2 hyperbolic curve, and by plotting Ve versus 15] showing straightline. Youcan ako show that she orginal versus (S) Sata Yield the same Ke value regardies of sch Saluer arg subsckuted into the Michaelis ‘Menten equation, (€) D013 ia 2. (@)O.107 pmote ter min.) mes ter Denia”, fe) 3TT ames Ttee"

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