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Biochemistry (review) Potato + soy bean + iodine =

bluish black
Cysteine - predominant amino acid (Starch) - (+) in iodine
in keratin Cross Linking
Prokaryotes – no compartment • Enzyme – Glycyl Oxidase
Aromatic Amino acid • Cofactor – Copper
• Phenylalanine Essential Amino Acids
• Tyrosine • Proline
• Tryptophan • Valine
Glycosilation • Threonine
• Glucose • Tryptophan
• Galactose • Isoleucine
Potato + saliva + Fehling’s reagent • Methionine
= Brick • HIstidine
Red • Arginine
Precipita
• Leucine
te
Prokaryotes are haploid • Lysine
Integral Proteins – Intraverses the Hydroxylation
whole membrane • Enzymes – Lysyl Hydroxylase
-- serves as channels Proline Hyroxylase
Acidic amino acids at Neutral pH – • Cofactor – Vitamin C /
negative ascorbic acid
Basic amino acid at Neutral pH – Minor Adult Hemoglobin – 2 alpha
positive and 2 delta
Phosphate groups (enzymes) Peroxisome – processing of alcohol
• Protein Kinase • Peroxidase enzyme
• Protein Phosphatase • Oxidase enzyme
Non-enzymatic – heat + strong acid 4 Types of Collagen
or base • Type I – skin and bone
Glysine – smallest amino acid • Type II – cartilage
Smooth endoplasmic reticulum – • Type III – Blood Vessel
lipid synthesis • Type IV – Basement
Cytoplasm – DNA of prokaryotes membrane
Glycine – in-optically active Milion’s Test – Phenol group w/c is
because it only has 2 present in Tyrosine
hydrogen groups (not a chiral Basic Amino Acid – proton donor
carbon) Acidic Amino Acid – proton
Chiral Carbon – 4 hydrogen group acceptor
Peripheral protein – surface of cell Enzymatic Cleavage – Trypsin
and can act as enzyme Chemical Cleavage – Cyanogen
Non – competitive Inhibitor – it Bromide
binds to the other side Potato + Hydrogen Peroxide –
• Vmax – decrease bubbles / foam
• Km – no change Competitve Inhibitor
• Km – increase • Chemical Group – Peptide
• Vmax – no change Bond
Predominant amino acids in elastin • (+) result – Violet
(small Myoglobin
nonpolar AA) P50 – 1 mmhg
• Glycine Hemoglobin
• Alanine P50 – 26 mmhg
• Valine Shift to the left
Hydrogen peroxide + Potato + • ↓ CO2
100°C = no foam • ↑ pH
-because the enzymes are • ↓ temp
destroyed at a very high • ↓ H+
temperature • ↓ 2,3 BPG
Bonds stabilizes the Tertiary • ↓ P50
Structure • ↑ O2
• Ionic Bond • ↑ affinity
• Hydrogen Bond Increases Velocity
• Hydrophobic Bond • ↑ substrate
• Disulfide Bond • ↑ temperature but not too
Phenolphthalein high
• Acid = colorless • pH depending on enzyme
• Basic = Pink because they have their own
Actions: optimal activity
• Ligase – formation of bonds Xanthoproteic Test
• Transferase – transfer Amino Acid that give a (+) result
• Lyase – removal of bonds • Tyrosine
Cytosol – Fluid content of • Tryptophan
cytoplasm * only activated aromatic rings are
Edman’s Reagent – labels the N- detected by tyrosine and
terminal tryptophan
Characteristics of peptide bond Trypsin cleaves Lysine and Arginine
• Partial Double bond Characteristics of Enzymes
• Rigid and planar • Specificity
• Trans configuration • Active site
• Unchared but polar • Regulated
Indole group w/c is present in • Cofactors
Tryptopha • Catalytic Efficiency
n – gives • Location
a (+) Reaction of Calcium Hydroxide
positive • Mouthwash – basic
result in • Vinegar – Acidic
Hopkin’s Reaction catalyses Urease
test
• Substrate – Urea (soy
Biuret’s test:
bean)
• Product - Ammonia
Henderson – Hasselbalch Equation
pH = pka + log [H −] – weak acid
or conjugate base
[HA]
Reaction catalyze by the enzyme
Amylase (saliva)
• Substrate – Starch
• Product – Simple sugar
Catalase
• Substrate – Hydrogen
Peroxide
• Product – H2O2 + O2