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PRCC_4MT-P1

Total questions: 157

Worksheet time: 1hrs 19mins

Name
Class
Date
1.
Purine catabolism
a)
Creatine
b)
Blood Uric Acid
c)
Blood Urea Nitrogen
d)
Bilirubin
2.
>95% exists as monosodium urates
a)
Creatine
b)
Blood Uric Acid
c)
Blood Urea Nitrogen
d)
Bilirubin
3.
98 to 99% are reabsorbed in the proximal convoluted tubules (PCT)
a)
Creatine
b)
Blood Uric Acid
c)
Blood Urea Nitrogen
d)
Bilirubin
4.
Blood Uric acid becomes _ in liver damage
a)
High
b)
Low
5.
leukemia
a)
Increased nuclear metabolism and cell turn over
b)
Other causes of hyperuricemia
c)
Decreased uric acid (hypouricemia)
6.
hemolytic disease
a)
Increased nuclear metabolism and cell turn over
b)
Other causes of hyperuricemia
c)
Decreased uric acid (hypouricemia)
7.
lymphoma
a)
Increased nuclear metabolism and cell turn over
b)
Other causes of hyperuricemia
c)
Decreased uric acid (hypouricemia)
8.
multiple myeloma
a)
Increased nuclear metabolism and cell turn over
b)
Other causes of hyperuricemia
c)
Decreased uric acid (hypouricemia)
9.
polycythemia
a)
Increased nuclear metabolism and cell turn over
b)
Other causes of hyperuricemia
c)
Decreased uric acid (hypouricemia)
10.
megaloblastic anemia
a)
Increased nuclear metabolism and cell turn over
b)
Other causes of hyperuricemia
c)
Decreased uric acid (hypouricemia)
11.
glycogen storage disease
a)
Increased nuclear metabolism and cell turn over
b)
Other causes of hyperuricemia
c)
Decreased uric acid (hypouricemia)
12.
lead poisoning
a)
Increased nuclear metabolism and cell turn over
b)
Other causes of hyperuricemia
c)
Decreased uric acid (hypouricemia)
13.
toxemia of pregnancy (low excretion)
a)
Increased nuclear metabolism and cell turn over
b)
Other causes of hyperuricemia
c)
Decreased uric acid (hypouricemia)
14.
ethanol and lactic acidosis
a)
Increased nuclear metabolism and cell turn over
b)
Other causes of hyperuricemia
c)
Decreased uric acid (hypouricemia)
15.
hormonal problem (common in menopausal women since estrogen aids in monosodium urate's production).
a)
Increased nuclear metabolism and cell turn over
b)
Other causes of hyperuricemia
c)
Decreased uric acid (hypouricemia)
16.
Fanconi syndrome
a)
Increased nuclear metabolism and cell turn over
b)
Other causes of hyperuricemia
c)
Decreased uric acid (hypouricemia)
17.
Wilson's Disease
a)
Increased nuclear metabolism and cell turn over
b)
Other causes of hyperuricemia
c)
Decreased uric acid (hypouricemia)
18.
Hodgkin's disease
a)
Increased nuclear metabolism and cell turn over
b)
Other causes of hyperuricemia
c)
Decreased uric acid (hypouricemia)
19.
Severe liver disease
a)
Increased nuclear metabolism and cell turn over
b)
Other causes of hyperuricemia
c)
Decreased uric acid (hypouricemia)
20.
Chemotherapy with 6-mercaptopurine or Azathioprine
a)
Increased nuclear metabolism and cell turn over
b)
Other causes of hyperuricemia
c)
Decreased uric acid (hypouricemia)
21.
Overtreatment with allopurinol
a)
Increased nuclear metabolism and cell turn over
b)
Other causes of hyperuricemia
c)
Decreased uric acid (hypouricemia)
22.
Is it required to fast when testing for Uric acid?
a)
Yes
b)
No
c)
Maybe
d)
Depends
23.
When using heparinized plasma, serum, or urine, uric acid would be stable for how many days?
a)
1 day
b)
2 days
c)
3 days
d)
4 days
24.
Uric acid is stable in both serum and urine for how many days at room temperature?
a)
1 day
b)
2 days
c)
3 days
d)
4 days
25.
Urine collection when testing for uric acid must be in what pH level?
a)
Acidic <7 pH
b)
Alkaline pH at 8
26.
Which of the following should not be used for Uric acid study?
a)
Heparin
b)
Sodium fluoride
c)
EDTA
d)
Sodium heparin
27.
Chemical method; its principle is colorimetry
a)
Caraway method
b)
Uricase method
c)
Uricase (coupled enzyme method)
d)
Isotope dilution mass-spectrometry
28.
Most common method BUT lacks specificity
a)
Caraway method
b)
Uricase method
c)
Uricase (coupled enzyme method)
d)
Isotope dilution mass-spectrometry
29.
Protein-free filtrate -> uric acid + phosphotungstic acid -alkaline solution -> tungsten blue
a)
Caraway method
b)
Uricase method
c)
Uricase (coupled enzyme method)
d)
Isotope dilution mass-spectrometry
30.
chemical method; NOT SPECIFIC!!!!!!
a)
Caraway method
b)
Uricase method
c)
Uricase (coupled enzyme method)
d)
Isotope dilution mass-spectrometry
31.
simplest and most specific method <3<3<3
a)
Caraway method
b)
Uricase method
c)
Uricase (coupled enzyme method)
d)
Isotope dilution mass-spectrometry
32.
Principle: uric acid + uricase --> oxidation (ALLANTOIN) + H2O2
a)
Caraway method
b)
Uricase method
c)
Uricase (coupled enzyme method)
d)
Isotope dilution mass-spectrometry
33.
Reference range: Males = 3.5 to 7.2 mg/dL Females - 2.6 to 6 m/dL
a)
Caraway method
b)
Uricase method
c)
Uricase (coupled enzyme method)
d)
Isotope dilution mass-spectrometry
34.
Decrease in absorbance is monitored at 293 nm
a)
Caraway method
b)
Uricase method
c)
Uricase (coupled enzyme method)
d)
Isotope dilution mass-spectrometry
35.
Uric acid = peak absorbance at 293 nm Allantoin = no absorbance at 293 nm
a)
Caraway method
b)
Uricase method
c)
Uricase (coupled enzyme method)
d)
Isotope dilution mass-spectrometry
36.
Uric acid -uricase -> allantoin & H2O2
a)
Caraway method
b)
Uricase method
c)
Uricase (coupled enzyme method)
d)
Isotope dilution mass-spectrometry
37.
H2O2 + chromogen -peroxidase -> oxidized chrmogen
a)
Caraway method
b)
Uricase method
c)
Uricase (coupled enzyme method)
d)
Isotope dilution mass-spectrometry
38.
Reference method
a)
Caraway method
b)
Uricase method
c)
Uricase (coupled enzyme method)
d)
Isotope dilution mass-spectrometry
39.
Uric acid (via uricase method)
a)
Peak absorbance at 293 nm
b)
No absorbance at 293 nm
40.
Allantoin (via uricase method)
a)
Peak absorbance at 293 nm
b)
No absorbance at 293 nm
41.
Males reference method in uricase // (uric acid)
a)
2.5 to 7.2 mg/dL
b)
3.5 to 7.2 mg/dL
c)
2.6 to 6 mg/dL
d)
6.2 to 6.2 mg/dL
42.
Females reference method in uricase // (uric acid)
a)
2.5 to 7.2 mg/dL
b)
3.5 to 7.2 mg/dL
c)
2.6 to 6 mg/dL
d)
6.2 to 6.2 mg/dL
43.
Specific biologic proteins that catalyze biochemical reactions without altering the equilibrium point of the reaction or being consumed or changed in composition. This is found in ALL body tissues as well.
a)
Carbohydrates
b)
Proteins
c)
Enzymes
d)
Lipids
44.
Lock and Key theory
a)
Emil Fischer
b)
Koshland
45.
They proposed that enzymes recognize their substrates as a lock receives a key. Basically, this theory states that enzymes have a specific shape that directly correlates to the shape of the substrate.
a)
Emil Fischer
b)
Koshland
46.
This model proposed that enzymes recognize their substrates as a lock receives a key. Basically, this theory states that enzymes have a specific shape that directly correlates to the shape of the substrate.
a)
Emil Fischer / Lock and Key theory
b)
Koshland / Induced fit theory
47.
According to this theory, binding of substrate to the enzyme brings a conformational change in the enzyme to either enhance or inhibit its activity.
a)
Emil Fischer / Lock and Key theory
b)
Koshland / Induced fit theory
48.
Induced fit theory
a)
Emil Fischer
b)
Koshland
49.
Where the substance on which the enzyme acts
a)
Active site
b)
Allosteric site
c)
Isoenzyme
d)
Cofactors or regulators
50.
A cavity other than the active site; - may bind regulator molecules
a)
Active site
b)
Allosteric site
c)
Isoenzyme
d)
Cofactors or regulators
51.
Enzyme exist in different forms within the same individual
a)
Active site
b)
Allosteric site
c)
Isoenzyme
d)
Cofactors or regulators
52.
nonprotein molecule, may be necessary for enzyme activity, that must bind to particular enzymes before a reaction occurs.
a)
Active site
b)
Allosteric site
c)
Isoenzyme
d)
Cofactors or regulators
53.
called "activators"
a)
Sodium (Na+)
b)
Calcium (Ca+)
c)
Magnesium (Mg+)
d)
Chloride (Cl-)
54.
Ca2+
a)
Metallic cofactor
b)
Nonmetallic cofactor
55.
Fe2+
a)
Metallic cofactor
b)
Nonmetallic cofactor
56.
Mg2+
a)
Metallic cofactor
b)
Nonmetallic cofactor
57.
Mn2+
a)
Metallic cofactor
b)
Nonmetallic cofactor
58.
Zn2+
a)
Metallic cofactor
b)
Nonmetallic cofactor
59.
K+
a)
Metallic cofactor
b)
Nonmetallic cofactor
60.
Br-
a)
Metallic cofactor
b)
Nonmetallic cofactor
61.
Cl-
a)
Metallic cofactor
b)
Nonmetallic cofactor
62.
Nicotinamide adenine dinucleotide
a)
Inorganic cofactor or activators
b)
Organic cofactor or coenzyme
c)
Holoenzyme
d)
Proenzyme or zymogen
63.
Serve as secondary substrates for enzymatic reactions
a)
Inorganic cofactor or activators
b)
Organic cofactor or coenzyme
c)
Holoenzyme
d)
Proenzyme or zymogen
64.
Coenzyme serve as secondary substrates for enzymatic reactions
a)
Inorganic cofactor
b)
Organic cofactor
c)
Holoenzyme
d)
Proenzyme or zymogen
65.
Prosthetic group: coenzyme + enzyme
a)
Inorganic cofactor
b)
Organic cofactor
c)
Holoenzyme
d)
Proenzyme or zymogen
66.
Nucleotide phosphate
a)
Inorganic cofactor
b)
Organic cofactor
c)
Holoenzyme
d)
Proenzyme or zymogen
67.
Vitamins
a)
Inorganic cofactor
b)
Organic cofactor
c)
Holoenzyme
d)
Proenzyme or zymogen
68.
a complete and active system
a)
Inorganic cofactor
b)
Organic cofactor
c)
Holoenzyme
d)
Proenzyme or zymogen
69.
inactive form of enzyme
a)
Inorganic cofactor
b)
Organic cofactor
c)
Holoenzyme
d)
Proenzyme or zymogen
70.
The first digit in the enzyme nomenclature is known as..
a)
Class
b)
Subclass
c)
Family
d)
Kingdom
71.
The second and third digits of the EC (enzyme commission) code number represents the __ and the ___ of the enzyme
a)
Class
b)
Subclass
c)
Family
d)
Subsubclass
72.
Function: Catalyze an oxidation - reduction
a)
Oxidoreductases
b)
Transferases
c)
Hydrolases
d)
Lyases
73.
Function: Catalyze the transfer of a group other than hydrogen
a)
Oxidoreductases
b)
Transferases
c)
Hydrolases
d)
Lyases
74.
Function: Catalyze the hydrolysis of various bonds
a)
Oxidoreductases
b)
Transferases
c)
Hydrolases
d)
Lyases
75.
Function: Catalyze the removal of groups from substrates without hydrolysis
a)
Oxidoreductases
b)
Transferases
c)
Hydrolases
d)
Lyases
76.
CO is an example of...
a)
Oxidoreductases
b)
Transferases
c)
Hydrolases
d)
Lyases
77.
LDH is an example of...
a)
Oxidoreductases
b)
Transferases
c)
Hydrolases
d)
Lyases
78.
MDH is an example of...
a)
Oxidoreductases
b)
Transferases
c)
Hydrolases
d)
Lyases
79.
ICD is an example of...
a)
Oxidoreductases
b)
Transferases
c)
Hydrolases
d)
Lyases
80.
G6PD is an example of...
a)
Oxidoreductases
b)
Transferases
c)
Hydrolases
d)
Lyases
81.
CK is an example of...
a)
Oxidoreductases
b)
Transferases
c)
Hydrolases
d)
Lyases
82.
AST is an example of...
a)
Oxidoreductases
b)
Transferases
c)
Hydrolases
d)
Lyases
83.
ALT is an example of...
a)
Oxidoreductases
b)
Transferases
c)
Hydrolases
d)
Lyases
84.
OCT is an example of...
a)
Oxidoreductases
b)
Transferases
c)
Hydrolases
d)
Lyases
85.
GGT is an example of...
a)
Oxidoreductases
b)
Transferases
c)
Hydrolases
d)
Lyases
86.
GST is an example of...
a)
Oxidoreductases
b)
Transferases
c)
Hydrolases
d)
Lyases
87.
GP is an example of...
a)
Oxidoreductases
b)
Transferases
c)
Hydrolases
d)
Lyases
88.
Esterases is an example of...
a)
Oxidoreductases
b)
Transferases
c)
Hydrolases
d)
Lyases
89.
ACP is an example of...
a)
Oxidoreductases
b)
Transferases
c)
Hydrolases
d)
Lyases
90.
ALP is an example of...
a)
Oxidoreductases
b)
Transferases
c)
Hydrolases
d)
Lyases
91.
CHE is an example of...
a)
Oxidoreductases
b)
Transferases
c)
Hydrolases
d)
Lyases
92.
LPS is an example of...
a)
Oxidoreductases
b)
Transferases
c)
Hydrolases
d)
Lyases
93.
Trypsin is an example of...
a)
Oxidoreductases
b)
Transferases
c)
Hydrolases
d)
Lyases
94.
LAP is an example of...
a)
Oxidoreductases
b)
Transferases
c)
Hydrolases
d)
Lyases
95.
AMY is an example of...
a)
Oxidoreductases
b)
Transferases
c)
Hydrolases
d)
Lyases
96.
CHY is an example of...
a)
Oxidoreductases
b)
Transferases
c)
Hydrolases
d)
Lyases
97.
E1 is an example of...
a)
Oxidoreductases
b)
Transferases
c)
Hydrolases
d)
Lyases
98.
NTP is an example of...
a)
Oxidoreductases
b)
Transferases
c)
Hydrolases
d)
Lyases
99.
Function: Catalyze the interconversion of geometric, optical, or positional isomers
a)
Lyases
b)
Isomerases
c)
Ligases
100.
Function: Catalyze the removal of groups from substrates without hydrolysis
a)
Lyases
b)
Isomerases
c)
Ligases
101.
Function: Catalyze the joining of two substrate molecules
a)
Lyases
b)
Isomerases
c)
Ligases
102.
GSH-S is an example of..
a)
Lyases
b)
Isomerases
c)
Ligases
103.
TPI is an example of..
a)
Lyases
b)
Isomerases
c)
Ligases
104.
Glucose phosphate --- is an example of..
a)
Lyases
b)
Isomerases
c)
Ligases
105.
Ribose phosphate --- is an example of..
a)
Lyases
b)
Isomerases
c)
Ligases
106.
Glutamate decarbo------ is an example of..
a)
Lyases
b)
Isomerases
c)
Ligases
107.
Pyruvate decarbo------ is an example of..
a)
Lyases
b)
Isomerases
c)
Ligases
108.
Aldolase------ is an example of..
a)
Lyases
b)
Isomerases
c)
Ligases
109.
ACP
a)
Esterase
b)
Peptidase
110.
ALP
a)
Esterase
b)
Peptidase
111.
CHE
a)
Esterase
b)
Peptidase
112.
LPS
a)
Esterase
b)
Peptidase
113.
Trypsin
a)
Esterase
b)
Peptidase
114.
Pepsin
a)
Esterase
b)
Peptidase
115.
LAP
a)
Esterase
b)
Peptidase
116.
AMY
a)
Esterase
b)
Peptidase
117.
CHY
a)
Esterase
b)
Peptidase
118.
E1
a)
Esterase
b)
Peptidase
119.
NTP
a)
Esterase
b)
Peptidase
120.
Tryptophan------ is an example of..
a)
Lyases
b)
Isomerases
c)
Ligases
121.
Decarb------ is an example of..
a)
Lyases
b)
Isomerases
c)
Ligases
122.
ACP
a)
Esterase
b)
Peptidase
123.
ALP
a)
Esterase
b)
Peptidase
124.
CHE
a)
Esterase
b)
Peptidase
125.
LPS
a)
Esterase
b)
Peptidase
126.
Trypsin
a)
Esterase
b)
Peptidase
127.
Pepsin
a)
Esterase
b)
Peptidase
128.
LAP
a)
Esterase
b)
Peptidase
129.
AMY
a)
Esterase
b)
Peptidase
130.
CHY
a)
Esterase
b)
Peptidase
131.
E1
a)
Esterase
b)
Peptidase
132.
NTP
a)
Esterase
b)
Peptidase
133.
Physically bind to the active site
a)
Competitive inhibitors
b)
Noncompetitive inhibitors
c)
Uncompetitive inhibitors
d)
Inhibitors only
134.
Binds an enzyme at a place other than the active site
a)
Competitive inhibitors
b)
Noncompetitive inhibitors
c)
Uncompetitive inhibitors
d)
Inhibitors only
135.
The inhibitor binds to the ES complex
a)
Competitive inhibitors
b)
Noncompetitive inhibitors
c)
Uncompetitive inhibitors
d)
Inhibitors only
136.
Can be diminished if the sample will be DILUTED
a)
Competitive inhibitors
b)
Noncompetitive inhibitors
c)
Uncompetitive inhibitors
d)
Inhibitors only
137.
Same catalytic reaction but different structure
a)
Isoenzyme
b)
Coenzyme
c)
Cofactors
138.
class
a)
First digit
b)
Second digit
c)
Third digit
d)
Fourth digit (and final digit)
139.
subclass
a)
First digit
b)
Second digit
c)
Third digit
d)
Fourth digit (and final digit)
140.
Subsubclass
a)
First digit
b)
Second digit
c)
Third digit
d)
Fourth digit (and final digit)
141.
serial numbers specific to each enzyme in a subclass
a)
First digit
b)
Second digit
c)
Third digit
d)
Fourth digit (and final digit)
142.
enzyme optimum temperature
a)
4 degree Celsius
b)
22 degree Celsius
c)
37 degree Celsius
d)
-20 degree Celsius or 2 to 8 degree Celsius or room temperature
143.
enzyme storage temperature
a)
4 degree Celsius
b)
22 degree Celsius
c)
37 degree Celsius
d)
-20 degree Celsius or 2 to 8 degree Celsius or room temperature
144.
enzyme pH
a)
6 to 7
b)
7 to 8
c)
9 to 10
145.
Increase enzyme concentration
a)
Hemolysis
b)
Lactescence or milky specimen
146.
Decrease enzyme concentration
a)
Hemolysis
b)
Lactescence or milky specimen
147.
Causes of increased serum enzyme levels include removal, necrosis, cell permeability, and number of cells.
a)
True
b)
False
148.
Reaction depends on enzyme concentration
a)
Zero order reaction
b)
First order reaction
149.
Where enzyme concentrations are always performed
a)
Zero order reaction
b)
First order reaction
150.
Reaction depends on substrate concentration
a)
Zero order reaction
b)
First order reaction
151.
Enzymes are used as a reagent to measure a specific analyte
a)
Zero order reaction
b)
First order reaction
152.
Relationship between the velocity of an enzymatic reaction and substrate concentration. V = Vmax [S] / Km + [S]
a)
Michaelis Menten
b)
Michaelis Menen
c)
Mikaelis Mentin
d)
Lineweaver-Burk Plot
153.
An illustration of the reciprocal of the substrate concentration (x-axis, 1/S) and the reciprocal of the reaction velocity (y-axis, 1/V), in which both are components of the enzyme kinetics
a)
Michaelis Menten
b)
Michaelis Menen
c)
Mikaelis Mentin
d)
Lineweaver-Burk Plot
154.
Most commonly measured when measuring enzyme activity
a)
Substrate
b)
Product
c)
Coenzyme
155.
Preferred sample for measuring enzymatic activity
a)
Whole blood
b)
Serum
c)
Plasma
d)
Urine
e)
Sweat
156.
Leads to false decrease
a)
EDTA
b)
Heparin
c)
Fluoride
d)
Citrate
157.
Citrate, EDTA, and fluoride plasma leads to..
a)
False increase
b)
False decrease

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