BIOCHEMISTY

BOARD REVIEW
December 28, 2013
E 1. System of fluid filled A. Golgi apparatus
cisterns
D 2. contains the enzymes for B. Lysosome
pyruvate oxidation
A 3. Stacks of flattened sacks C. Nucleolus

B 4. Contains digestive D. Mitochondria

enzymes
5. site of ribosome E. Endoplasmic
C
assembly reticulum
Organelle Description Function

Ribosome Protein + RNA Site of protein

synthesis
Lysosomes bags containing which digest worn-
digestive enzymes out or non-usable
cell structures
Demolition sites

Peroxisomes Membrane Uses molecular O2

containing oxidase to detoxify harmful
enzymes subs
Converts free
radicals to H2O2
Organelle Description Function
Golgi apparatus stacks of flattened serves to modify and
sacks package proteins
a routing center for proteins
and modifies the
oligossacharide moieties of
glycoproteins.
Endoplasmic System of fluid Rough – CHON synt
reticulum (ER) Smooth – lipid syn & metabolism
filled cisterns
& detoxification
Mitochondria powerhouse of the contain the enzymes for citric
cell acid cycle, beta oxidation, and
respiratory chain
A 6. lipids that contain A. cerebrosides
carbohydrate, one fatty
acid and sphingosine, but
no phosphoric acid or
glycerol.
B 7. contain sphingosine, long- B. gangliosides
chain fatty acids, hexoses
and neuraminic acid.
C 8. Glycolipids C. Both A and B
Gaucher's disease
is the accumulation of
glucocerebrosides
B 9. This is the only reaction A. succinate to
coupled with substrate fumarate
level phosphorylation in
the TCA

A 10. This is the only reaction in B. succinyl CoA

TCA that involves to succinate
FAD/FADH2
 Glucose
2H
Pyruvic acid
CO2 + 2H (NAD) + 3 ATP
Acetyl coA

Oxaloacetic acid Citric acid

(3ATP) 2H NAD
Malic acid Cis- aconitic acid
+H2O +H2O
Fumaric acid Aerobic Isocitric acid
(2ATP) 2H
(FAD)
Stage or + H2O
2H (NAD) = (3 ATP)

Succinic acid Kreb’s cycle Oxalosuccinic acid

1 ATP CO2
Succinyl coA Alpha Ketoglutaric acid
CO2 2H (NAD) = (3ATP)
C 11. small, extrachromosomal A. Prions
circular DNA molecules proteinaceous
found in prokaryotes and infectious

B 12. The ability of certain B. Wobble

anticodons to pair with
codons that differ at the
third base

A 13. infectious agent that C. Plasmids

contains both proteins and Covalently closed
circular DNA
nucleic acid
Prions
DISEASES:
Cattle= bovine spongiform
encephalopathy(BSE, also known as
"mad cow disease")
Sheep= "scrapie”
humans = Creutzfeldt-Jakob disease
(CJD) in
C 14. Connect the nitrogen A. Hydrogen bond
bases
15. connect the 3' hydroxyl B. Glycosidic bond
A group of one pentose to
the 5 carbon of another
pentose

16. bond between the 1’ C. phosphodiester

B carbon of the sugar and bond
the base nitrogen
H- bond

phosphodiester bond
FUNDAMENTAL COMPONENTS:
 Pentose sugar
 DNA – deoxyribose
 RNA – ribose
 Difference: Carbon 2 only difference is
the presence of a hydroxyl group
 Phosphoric acid
 Responsible for acidic character of
nucleic acid
 Nitrogenous base
 PURINES – Guanine & Adenine
 PYRIMIDINES – Cytosine, Uracil, Thymine
DNA FORMS
 Z-DNA
 unique left – handed helical structure

A and B DNA are both right - handed

double helices
B – DNA
 most common / most abundant
 Described by Watson & Crick using X –
ray diffraction
 A – DNA
 less common
 dehydrated B – DNA form
Replication
1. Helicases open the DNA
double helix
2. Primase creates template
RNA primer for each strand
Replication
3. DNA polymerase synthesizes DNA in
a 5’ 3’ direction
Replication
4. DNA polymerase removes the RNA
primer and fills the gaps between
Okazaki fragments
5. DNA ligase joins the DNA fragments
of the lagging strand, creating a
single DNA molecule
Xeroderma pigmentosa

A genetic disease due to

defective mechanism of
pyrimidine dimmers
 17. Adenine binds to thymine, A. Antiparralel
B and cytosine binds to
guanine
C 18. One parent strand and one B. Complementarity
daughter strand appear in
the final product
D 19. 6 codon = 1 amino acids C. Semiconservative
manner
A 20. Each end of the DNA double D. Degeneration
helix contains, the 5' end of
one strand and the 3' end of
the other strand
E
21. holds the genetic information used for A. Introns
protein synthesis
A 22. noncoding regions that alternate with B. Primer
coding regions in the polypeptide
sequence
D 23. set of prokaryotic structural genes, which C. Okazaki
are transcribed as a unit fragments
24. discontinuous stretches in which the D. Operon
C lagging strand is initially synthesized
during DNA replication

B
25. A short piece of nucleic acid (DNA or E. Sense strand
RNA), base paired with a DNA template
strand and provides a free 3'-OH end from
which DNA polymerase can extend a DNA
strand.
D
26. metabolic disorder affecting A. phenylketonuria
branched-chain amino acids
C 27. Deficiency of exonuclease B. alkaptonuria

A
28. Absence of phenylalanine C. Xeroderma
hydroxylase pigmentosa

B 29. Deficiency of homogentisate D. Maple syrup urine

oxidase disease
E 30. oxidation of heme protein in E. Methemoglobine
hemoglobin mia
D
31.
Amino acid with imino A. Arginine
group
B 32.
With hydroxyl group B. Serine
F 33.
With sulfur atom C. Glutamine

A Basic amino acid

34.
D. Proline

E Without chiral carbon

35.
E. Glycine

C Neutral amino acid

36.
F. Cysteine
 Basic Amino Acid Structure
carboxyl group
 a-carbon is chiral
(except for glycine)
amino group
 at pH 7.0 uncharged
amino acids are
zwitterions
 amino acids have a
tetrahedral structure a-carbon
side chain
 Aromatic Amino Acids
Phenylalanine (Phe, F)
Tyrosine (Tyr, Y) – -OH ionizable (pKa =
10.5), H-Bonding
Tryptophan (Trp, W) – bicyclic indole
ring, H-Bonding
Sulfur Containing Amino Acids

 Methionine (Met, M) – “start” amino

acid

 Cysteine (Cys, C) – sulfur in form of

sulfhydroyl, important in disulfide
linkages, weak acid, can form
hydrogen bonds.

 Cystine is a dimer of cysteine

Acidic Amino Acids
• Negatively charged at physiological pH

• Aspartate –

• Glutamate –
Basic Amino Acids
 Positively charged at physiological pH
 Histidine – imidazole ring protonated/ionized, only
amino acid that functions as buffer in physiol range.
 Lysine - diamino acid
 Arginine - guianidinium ion, most basic amino acid
isoelectric point (pI)
isthe pH at which a particular
molecule or surface carries no net
electrical charge

Ata pH below their pI, proteins

carry a net positive charge
Above their pI they carry a net
negative charge
A
37. order of amino acids in the A. Primary
polypeptide chain
38. overall arrangement and B. Secondary
C
interrelationship of various
region
D 39. arrangement of polypeptide C. Tertiary
chains in rotation to one
another in a multi-chained
protein
B 40. spatial arrangements of amino D. Quaternary
acid residues close to one
another in the linear sequence
of a polypeptide chain
Primary Structure
An order of w/c amino acids are
joined together, and it includes the
location of any disulfide bonds

peptide bond - is the covalent

amide linkage that joins aa in a
protein
 Secondary Structure
Configuration
Refers to geometric relationship
between a given set of atoms
Conformation
Refers to the three – dimensional
architecture of a protein, the spatial
relationships of all atoms to all the
others
Secondary Structure

regularly repeating local

structures stabilized by
hydrogen bonds.

alpha helix and beta sheet

Tertiary Structure
 the overall shape of a single protein
molecule
 the spatial relationship of the secondary
structures to one another.
 stabilized by nonlocal interactions, most
commonly the formation of a
 hydrophobic core, but also through salt
bridges,
 hydrogen bonds,
 disulfide bonds, and
 even post-translational modifications.
 fold.
Quaternary Structure
 proteinsubunits
 assembly or protein complex.
 Contain two or more polypeptide chains
associated by non – covalent forces
 Multimeric proteins

 The bonds linking the quaternary structure are

 all noncovalent-hydrogen bonds,
 electrostatic/salt bonds,
 and hydrophobic bonds
A 41. Precursor of serotonin A. Tryptophan

C 42. Precursor of histamine B. Tyrosine

B 43. precursor in the synthesis C. Histidine

of these catecholamines
tyrosine
 May be converted to fumaric acid,
adrenaline (cathecolamines), tyramine and
melanin
 4-hydroxyphenylalanine
 found in large quantities in casein.
Histamine
 formed by the decarboxylation of
histidine.
 It is also a powerful vasodilator.
 secreted by mast cells as a result of
allergic reactions or trauma
B 44. most abundant single protein A. Elastin
in vertebrates

A 45. important structural B. Collagen

component of arterial blood
vessels and ligaments

C 46. major proteins of skin and C. Keratin

hair
D 47. Fibrous protein/s D. All of the
choices
D 48. Albuminoid/s
B 49. glycoproteins A. simple proteins

A 50. Glutenin in wheat B. conjugated proteins

D 51. Peptones C. primary derived
proteins
C 52. Fibrin from D. Secondary derived
fibrinogen proteins
B 53. Casein in milk
C 54. proteins formed during the early stages of
protein hydrolysis by means of acid or alkali
B 55. proteins that are combined in nature with
some nonprotein substances
 The SIMPLE PROTEINS an listed in
the following table
TYPE EXAMPLE OR OCCURENCE
Albumin -ovalbumin in egg
-serum albumin in blood
globulins -serum globulin
glutelins -glutenin in wheat
prolamines -zein in corn
albuminoids -keratin in hair and horny tissue
-elastin in tendons ad arteries
-collagen in skin and tendons

histones -histones and hemoglobin

protamines -salmin and sturin In fish sperm
 Types of CONJUGATED PROTEINS
TYPE EXAMPLE / OCCURRENCE
phosphoprotein -casein in milk
-ovovitellin in egg yolk
nucleoprotein -nuclein in cell nuclei
glycoproteins -mucins in vitreous humor ad saliva

chromoproteins -hemoglobin in blood and flavoproteins

lipoproteins -Fatty acids, sterol and lecithin

metalloproteins -Tyrosinase (Cu), arginase(Mn),
xanthine oxidase (Mo)
Primary Derived Proteins
TYPE EXAMPLE/OCCURRENCE

proteans fibrin from fibrinogen

myosan from myosin
Metaproteins acid and alkali albuminates
Coagulated Coagulated albumin
Proteins Cooked meat
Secondary derived proteins
substances formed during the
progressive hydrolysis of proteins.

subclassification
proteoses (highest molecular weight group)
peptones (lower molecular weight than proteoses)
peptides (small hydrolytic fragments 2-20 amino acids)
B 56. Thiamine A. Peripheral
neuropathy

D 57. Riboflavin B. Wernicke-Korsakoff

syndrome

A 58. Pyridoxine C. Pellagra

E 59. Folic acid D. Cheilosis

C 60. Niacin E. Megaloblastic anemia

Thiamine deficiency
 BERIBERI

 dry beriberi - which manifest as

paralysis and cardiac failure, lower
extremity edema and muscle pain

 wetberiberi - edema begins on feet

and ascends.

 Wernicke Korsakoff syndrome

B 61. nonsuperimposable mirror
A.
Isomers
images of each other
D 62. Glyceraldehyde and
B.
Enantiomer
Dihydroxyacetone
C 63. differing only in the
C.
Anomers
configuration of the
substituents on the carbonyl
carbon
B 64. D-threose and L-threose D.
Tautomers
A 65. Glucose, fructose and galactose E
.
Epimers

E 66. glucose and Galactose

 Stereochemistry
Three main groups:

 optical isomer
 ENANTIOMER – D and L forms
 DIASTEREOISOMER - Epimers
 geometric isomers
 Cis and Trans
 conformational isomers
 Boat and Chair
 epimers
 differsonly in the configuration of their hydroxyl
group at middle carbons
 Ex: Glucose epimers

Mannose : C2
Galactose : C4
EPIMERS
ANOMERS
ENANTIOMERS
D 67. Glycosaminoglycan A. hyaluronic acid

68. structural constituent of B. Chondroitin

C
exoskeletons

C 69. N-acetyl-Beta-D- C. Chitin

glucosamine

A 70. Spreading factor D. A and B

D 71. cleaves a carbon to carbon A. isomerases
bond to create an aldehyde
group

E 72. Hydrolase B. Lyase

B 73. Decarboxylase C. reductase

A 74. Racemase and Mutase D. Aldolase

C 75. adds hydrogen atoms to a E. Esterase

molecule
B 76. most important in controlling A. Pyruvate
glycolysis kinase
77. catalyzing the reaction of glucose B. Phosphofruct
C to glucose-6-phosphate okinase

E 78. catalyze irreversible steps in C. hexokinase

glycolysis

B 79. catalyzes the conversion fructose- D. citrate

6-P to fructose-1,6-bis-P synthase

D 80. catalyzes the conversion of Acetyl- E. A, B and C

CoA and Oxaloacetate to citrate only
81. key enzyme that links glycolysis,
A TCA cycle, amino acid metabolism
C 82. pyruvate carboxylase A. bypass the
hexokinase reaction
B 83. fructose B. bypass the PFK
biphosphatase reaction
A 84. glucose-6-phosphatase C. bypass the,
pyruvate kinase
reaction of
glycolysis
C 85. PEP carboxinase
Glycolytic enzymes Gluconeogenic enzymes

- Glucokinase - Glucose 6 Phosphatase

- Phosphofructose - Fructose biphosphatase
isomerase - PEP carboxykinase
- Pyruvate kinase - Pyruvate carboxylase
 IDENTIFICATION TESTS:

C 86. Resorcinol A. Moore’s test

87. Alpha naphthol B. Xanthoproteic acid

E
88. NaoH C. Seliwanoff’s test
A
B 89. Nitric acid D. Osazone test

D 90. Phenylhydrazine E Molisch test

 REAGENT COMPOSITION

C
91.
Bismuth subnitrate, KOH, A. Fehling’s
Rochelle’s salt reagent
92.
Cupric acetate with acetic B. Benedict’s
D
acid reagent
E 93.
Ammoniacal silver nitrate C. Nylander’s
reagent
94.
B CuSO4, Na2CO3, Na citrate D. Barfoed’s
reagent
A
95.
CuSO4, NaOH, Rochelle’s salt E. Tollen’s reagent
Molisch test
AKA: alpha naphtol reaction
a nonspecific test for
carbohydrates.

This reaction is due to the formation

of furfural and furfural derivatives

Acid utilized: Sulfuric acid

 Seliwanoff’s test
 Test for ketose
 differentiating test for aldose and ketose

 Reagents:
 Conc. HCl and resorcinol

 RED coloration (ketose)

Tauber’s test

Test
for ketoses
AKA: aminiguanidine reaction

(+) result: bright reddish purple

 Reducing PROPERTY OF
SUGARS
1. Benedict’s test
 the traditional test for glucose in the urine
 reduction of cupric ions to cuprous oxide
 Reagents:
 CuSO4, Na2CO3, and sodium citrate
 ADVANTAGE over Fehling’s rgt: weaker
alkalinity provides more sensitivity than
Fehling’s soln, Stable soln
 BRICK RED PPT
 Reduction test
2. Fehling's test
 Reagents:

 Fehling’s A :CuSO4 – oxidizing agent

 Fehling’s B:
Rochelle’s salt – prevents precipitation of
copper as Cu(OH)2
NaOH – makes the sugar more reactive
 brick red precipitate
Bial’s test
Confirmatory test for Pentoses

(+) result: Blue-green

 Reactions of sugars with
phenylhydrazine
 Sugar + Phenylhydrazine
= yellow ppt
 OSAZONE formation – OZONE formation

 Mannose forms an insoluble white phenylhydrazone

readily
D
96. Salkowski reactions A. Aminoguanidine reaction

A 97. Tauber’s test B. Alpha naphthol reaction

B 98. Molisch test C. Triketohydrindene hydrate
F 99. Tollen’s test D. Cherry red color
C 100. Ninhydrin test E. Violet color

J
101. Xanthoproteic test F. Silver mirror
H 102. Moore’s test G. Red color
E 103. Biuret test H. Brown color
G 104. Sakaguchi test I. Green

I
105. Liebermann-Burchard J. Yellow
test
 106. A. Aminoguanidine reaction
G Purple ring at the
junction
B 107.
Brick red ppt B. Fehling’s test

F 108.
Deep blue C. Anthrone test
109.
A Bright reddish D. Millon’s test
purple
C 110. Blue-green color E. Moore’s test
D 111.
Flesh to red F. Iodine test
J 112. Black ppt G. Molisch test
E 113. Brown color H. Hopkin’s cole test
H 114. Purple I. Osazone test
I 115. Yellow ppt
116.
Prosthetic groups in lipids H Osmic test
L Iodine test
117.
Glycogen
118.
Reducing sugars
119.
N Nylander’s test
Galactose
120.
A Mucic acid test
Arginine
Q Sakaguchi test
121.
Cerebrosides
122.
D Lassaigne’s test
Differentiates aldoses from
ketoses
C Seliwanoff’s test
123.
Differentiates mono from
J Barfoed’s test
disaccharides
124.
Cholesterol T Salkowski test & LB test

125.
Choline F Rosenheim’s test
126. Peptide linkages F Biuret test
R Basic lead test
127. Sulfur containing amino acid
128. Tryptophan
P Ehrlich & HC test
129. Free amino group E Ninhydrin test
130. Cysteine
P Basic lead test
131. General test for
carbohydrates
I Molisch test
Xanthoproteic
K
132. Detects the presence of
benzene ring test
133. Test for steroidal nucleus G Liebermann – Burchard

134. Cystine
P Basic lead test
135. Tyrosine K Xanthoproteic test
136.
Calciferol C Vitamin D
F Vitamin B1
137.
Thiamine
138.
Anti-scorbutic vitamin
B Vitamin C
139.
Pyridoxine J Vitamin B6
140.
Cobalamin L Vitamin B12
141.
Anti-sterility vitamin D Vitamin E
142.
Chick anti-dermatitis
factor I Vitamin B5
143.
Ascorbic acid B Vitamin C
144.
Laetrile M Vitamin B17
145.
Retinol A Vitamin A
146.
Panthotenic acid I Vitamin B5
147.
Biotin N Vitamin H
O Vitamin P
148.
Permeability factor
149.
Anti-hemorrhagic factor E Vitamin K
150.
Alpha tocopherol D Vitamin E
151.
Rutin and Hesperidin O Vitamin P

G Vitamin B2
152.
Riboflavin
K Vitamin B9
153.
Folic acid

H
154.
Niacin
Vitamin B3
155.
Phytonadione E Vitamin K
 VITAMIN K
K1- Phytonadione
K2 – Menaquinone
K3 – Menadione - most active synthetic
form
K4 – Menadiol

ANTI-HEMORRHAGIC FACTOR
 Alpha 1 Chemical name of lactic acid
hydroxypropionic
acid

2 Random coils and triple helices

Secondary
are examples to what protein
structure?
3 Results from gamma
Alanine
carboxylation of aspartic acid
4 Compound of protein with a
Chromoprotein
pigment component
Tautomerization 5 Action of diluted alkali on sugars
Glyceraldehyde6 The simplest monosaccharide

Oxaloacetate 7 Citrate can be formed from the

combination of Acetyl CoA with
_________
Urea 8 Uremia refers to the build up of
____ in the kidney
propenal 9 IUPAC name of acrolein

Zwitterions 10 Amino acid at an isoelectric point

exists as___
 11 What test utilized resorcinol and
Seliwanoff’s
acid to react with sugar forming
test
furfurals?
AUG 12 Start codon

3 13 How many hydrogen bonds are

formed between cytosine and
guanine?
14 The inactive form of enzyme
Zymogens

12 15 How many ATPs are produced for

every oxidized acetyl CoA?
 16
This type of mutation occurs when
Nonsense
the codon containing the changed
base may become a termination
codon
17
HCl is needed in the activation of
Pepsinogen
pepsin from what inactive substance?
Zein 18
An official simple protein from corn
19
Chair The chemical representation shows
the most stable conformation of
conformation
hexoaldopyronoses
20
Site of conversion of beta carotene to
Small intestine
vitamin A
 21
Cabbage and cauliflower are good
K sources of what vitamin?
22
The principal energy-carrying
ATP
molecule in a cell
Peptide bonds 23
Bond between 2 amino acids
24
This test distinguishes between
Barfoed’s reducing sugar monosaccharides
test and reducing disaccharides based
on the difference in the rate
reaction
25
60 -90 mg in 100 The amount of glucose present in
mL of blood human blood
 26 Phosphoprotein found in egg
Vitelin yolk

Mannose 27 C2 epimer of glucose

28 This is also known as RNA-

Reverse directed polymerase
transcriptase
29 The group of lipids which is
Phospholipids
considered amphipathic

Sulfuric acid 30 Dehydrating agent in Molisch

reagent
 31 The enzyme catalyzes the
PFK
conversion fructose-6-P fructose-
1,6-bis-P
32 This is known as the Embden-
Glycolysis
Meyerhof pathway.
33 Also known as Alpha-naphthol
Molisch test
reaction
34 Vitamin used in Wernicke-
Thiamine
Korsakoff syndrome
35 Solution used to ascertain degree
Hubl’s solution
of unsaturation
Ethanolamine 36 Removal of carbon dioxide from
serine can form what substance?

Trp 37 Amino acid precursor of serotonin

38 The process of biosynthesis of
Gluconeoge glucose from non-carbohydrate
nesis precursors
Maple syrup 39 Disease associated with
urine dse deficiency of branched chain
amino acids.
Megaloblastic 40 Folic acid defiency results to what
anemia type of anemia?
Process of removing glucose from
blood
Glycolysis
Anaerobic oxidation
Glucose oxidation for heat and
energy

Glycogenesis
Synthesis of glycogen from
glucose in the liver and muscles
 Process of adding glucose to
blood
 Gluconeogenesis
 Synthesisof blood glucose in the liver from
non-carbohydrate sources (amino
acids,lactic acids)
 Takes place in the liver and kidneys
 Glycogenolysis
 Conversion of liver glycogen to glucose
 41 Specific test for galactose, due to
Mucic acid
the formation of highly insoluble
test
crystals
RBC 42 Cellular elements of the blood
devoid of nucleus
Rosenheim’s 43 Test used to detect the presence of
test choline
Cytoplasm 44 Site of anaerobic glycolysis

Rennealing 45 It is the phenomena of renaturation

of nucleic acid after it has been
subjected to high temperature then
to room temperature
 46 The essential amino acids used in
Trp
the synthesis of niacin

Glucose 47 It is the most abundant hexose

inside the body
Sakaguchi 48 Specific test for Arginine
test
49 Process of converting liver
Glycogenol glycogen to glucose
ysis
50 The sugar involved in DNA
Deoxyribose
Reticuloendoth 51 Site for the metabolic
elial cells degradation of hemoglobin

Golgi 52 Stacks of flattened sacks refers to

apparatus what part of the cell?
homogentisate53 Enzyme deficient in alkaptonuria
oxidase
54 Accumulation of
Gaucher’s
glucocerebrosides results to what
disease
condition?
55 proteins that are combined in
conjugated nature with some nonprotein
proteins
substances
 56 most important in controlling
Phosphofruc
glycolysis
tokinase
Protamines 57 Simple protein that is soluble in
70% alcohol
58 This enzyme is responsible for
DNA
removing the RNA primer on
polymerase
DNA.
59 A non – pentose sugar which is
cellobiose
also positive for Tollen’s
phloroglucinol test
Gamma 60 Aspartic acid can be converted to
decarboxylation alanine through what process?
 61 Protamine in mackerel
Scrombine

Cretinism 62 Hypothyroid condition in children

63 Metal present in carbonic

Zinc anhydrase
64 Basic unit of collagen
Tropocollagen

65 Also called aminoguanidine

Tauber’s test
reaction
 66 Tryptophan deficiency caused by
Hartnup’s
defective reabsorption in the
disease
kidneys
Glucose 6- 67 Used to bypass hexokinase
phosphatase
reaction
Lecithin 68 Phospholipid from soybean

69 N-acetylgalactosamine refers to:

Chondroitin

furfural 70 Action of acids on pentose sugar

can form___
copper 71 The metal present in Tyrosinase
 Deficiency
state
B3 Pellagra Occur in pt whose diets are
(niacin) deficient in niacin and Trp

Hartnup’s Defect in the intestinal and renal

disease reabsorption of neutral amino
acids (Trp), Trp is lost in urine
and feces

Carcinoid Excessive utilization of Trp due

syndrome to its use in the synthesis of
serotonin, w/c produces flushing
and diarrhea.
 72 The site of acylglycerol synthesis
ER
Hexoaminidase 73 The enzyme deficient in patients
A with Tay-Sachs disease
74 This mediates the first step the
HMG-coA synthesis of sterol.

Raffinose/ 75 An important non-reducing

melitose trisacchiride

Osazone test/ 76 Other name of Kowarsky test

phenylhydrazine

pH of the solution 77
Difference between Benedict’s and
Barfoed’s test reagent
 78 Principal site for the synthesis of
liver
urea

denaturation 79 Breakage of the hydrogen bonds

in proteins refers to what
process?
80 What is the anti – codon in the
UGC tRNA that corresponds to the
codon ACG in mRNA?
True or False
 1. Phenylalanine, Leucine and tyrosine
T
are ketogenic amino acid
2. Insulin promotes exocytosis of glucose
T
transporters in the skeletal muscles
3. The difference between intake the
T output of nitrogenous compounds is
known as nitrogen balance
4. Negative nitrogen balance results
F
when there is too much protein intake
5. In a healthy adult, nitrogen balance is
T in equilibrium when intake equals
output
 Positive nitrogen balance occurs
F when dietary intake is less than
excretion of nitrogenous compounds
7.
Leucine, isoleucine and Valine are
T examples of branched chain amino
acids.
8.
Purple color at the junction is the
F Yellow
positive result for xanthoproteic test
F 9.
Glucose and fructose are epimers.
Geometric isomers
10.
T Principle involved in the isolation of
casein in milk is by isoelectric
precipitation
 11. Biuret test is used to identify
F the presence alpha amino
Peptide linkages acids.
12. Nitrogen base and sugar are
T
the components of nucleosides
13. Beta oxidation of fatty acids
F
Mitochondria occurs in the ribosomes
14. Building blocks of RNA and DNA
F are the hexoses
Purines and Pyr
15. Linoleic acid is an omega-3 fatty
T
acid
F 16. The end product in the hydrolysis
glucose of glycogen is galactose
17. When starches are heated they
F dextrins produce dextran
18. Osazone test is also known as
F kowarsky Trommer’s test
19. The only optically inactive amino
F acid is Lysine
glycine
20. Sweet taste of a compound is
F generally attributed to presence of
OH ions
cations
T 21. Glutamine is a neutral amino acid

22. Hormones are chemical

T messengers
23. Capric acid contains 12 carbons
F 10

24. Iron is located at the center of the

F
heme cyclic tetrapyrole known as
hemoglobin
25.
F negative Histidine is positive for Sodium
nitroprusside
F 26. Protein digestion starts in the
stomach mouth
27. Mutarotation is a process of
T interconversion between the alpha
and beta forms, using the open-
chain structure as an intermediate.
28. Collagen is a globular protein
F fibrous
F AUG 29. Codon for methionine is UAG

30. The principal end product f protein

F
UREA metabolism is uric acid