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CC2 LECTURE > ACP, ALP, AMYLASE, LIPASE, GGT > Flashcards

ACP, ALP, AMYLASE, LIPASE, GGT Flashcards

1
Q

belongs to the same group of phosphatase enzymes as ALP and is a hydrolase that catalyze the same reactions

A

ACP

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2
Q

Major difference between ACP and ALP is the pH where ACP activity takes place at a pH of

A

5.0 (acidic)

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3
Q

ACP is buffered at pH
ALP is buffered at pH

A

6
10.2

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4
Q

Belongs to a group of enzymes that catalyzes the hydrolysis of various phosphomonoesters in alkaline pH

A

ALP

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5
Q

Considered a non-specific enzyme, able to react with many different substrate

A

ALP

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6
Q

It liberates inorganic phosphate from an organic phosphate ester w/ the concomitant production of an alcohol

A

ALP

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7
Q

is required as an activator of ALP

A

Mg

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8
Q

GGT Chemical Name

A

Gamma-glutamyl transpeptidase

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9
Q

Catalyzes the transfer of y-glutamyl residue from y-glutamyl peptides to amino acids, other peptides, or H2O

A

GGT

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10
Q

Cell membrane-bound

A

GGT

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11
Q

Largest amounts found in the kidney

A

GGT

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12
Q

Small accumulations in the liver (hepatobiliary tree) and heart

A

GGT

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13
Q

GGT Half-life:

A

7 - 10 days

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14
Q

GGT In alcoholic liver disease:

A

28 days

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15
Q

AMS Chemical Name:

A

α-1,4-glucan-4-glucanohydrolase

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16
Q

Hydrolases are enzymes that catalyzes the breakdown of starch and glycogen

A

AMS

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17
Q

Starch is made up of both

A

Amylose and Amylopectin

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18
Q

-long unbranched chain of glucose linked by a,1-4 glycosidic bonds (glucose molecule)

A

Amylose

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19
Q

-branched chain polisaccharide with a,1-6 linkage (polysaccharide)

A

Amylopectin

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20
Q

a-AMS attacks only the a,1-4 glycosidic bonds to produce the degradation products:

A

o Glucose
o Maltose
o intermediate chain (Dextrin)

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21
Q

MW: 45,000 daltons

A
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22
Q

considered the smallest enzyme and can pass through glomerular filter

A
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23
Q

top of blood vessels located between the bowman’s capsule within the kidney

A

Glomerulus

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24
Q

microscopic filter”

A

Glomerulus

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25
Q

Blood filtration in the kidney where fluids, ions, glucose, and waste products are being removed from the glomerular capillaries

A

Glomerulus

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26
Q

AMS Metalloenzyme:

A

Calcium

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27
Q

Requirement for the functional integrity of amylase

A

Calcium

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28
Q

AMS Optimum pH:

A

6.9 – 7.0 in serum

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29
Q

Normal serum contains both AMS

A

salivary and pancreatic AMS

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30
Q

Normal amylase / creatinine ratio =

A

1.0% – 4.0% (0.01 – 0.04)

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31
Q

A:C ratio (Acute Pancreatitis) =

A

> 4.0% (up to 15%)

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32
Q

An elevated amylase-creatinine clearance ratio has been established as being highly specific for the diagnosis of

A

acute pancreatitis

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33
Q

Calculates the ratio of amylase to creatinine that if both filtered by the kidney

A

amylase-creatinine clearance ratio

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34
Q

LPS Chemical name:

A

Triacylglycerol Acylhydrolase

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35
Q

ACP SYSTEMATIC NAME

A

E.C. 3.1.3.2

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36
Q

ALP SYSTEMATIC NAME

A

E.C. 3.1.3.1

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37
Q

GGT SYSTEMATIC NAME

A

E.C. 2.3.2.1

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38
Q

AMYLASE SYSTEMATIC NAME

A

E.C. 3.2.1.1

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39
Q

LIPASE SYSTEMATIC NAME

A

E.C. 3.1.1.3

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40
Q

inhibited by tartrate

A

Prostatic ACP (band 1)

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41
Q

greatest activity in the prostate gland

A

Prostatic ACP (band 1)

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42
Q

fastest migrating ACP isoenzyme

A

Prostatic ACP (band 1)

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43
Q

2nd fastest migrating ACP isoenzyme

A

Bone - osteoclasts (band 5)

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44
Q

major form in plasma ACP

A

Platelets, RBCs & Monocytes (band 3)

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45
Q

Resistant to tartrate inhibition

A

Bone - osteoclasts (band 5)

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46
Q

differentiates prostatic fractions from, bone-osteoclast fractions in ACP

A

Inhibition

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47
Q

differentiates bone fractions from, liver fractions in ALP

A

Enzymes or lectins

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48
Q

Rate of mobility of ALP ISOENZYMES

A
  1. Liver isoenzyme – migrates the fastest
  2. Bone isoenzyme – 2nd
  3. Placental isoenzyme – 3rd
  4. Intestinal isoenzyme – 4th
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49
Q

Its activity starts in the salivary gland where it initiates the hydrolysis of starch while food is in the mouth and esophagus

A

S-type Isoamylase

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50
Q

Its action is terminated by the acidity of the stomach

A

S-type Isoamylase

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51
Q

Inhibited by monoclonal antibody

A

S-type Isoamylase

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52
Q

Inhibited by protein isolated from wheat

A

S-type Isoamylase

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53
Q

represent 2/3 of AMS activity of normal serum

A

S-type Isoamylase

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54
Q

Synthesized by the pancreatic acinar cells and secreted into the intestinal tract via the pancreatic duct system

A

P-type Isoamylase

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55
Q

Its action is favored by the mildly alkaline condition of the duodenum

A

P-type Isoamylase

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56
Q

Inhibited by monoclonal antibody

A

P-type Isoamylase

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57
Q

Inhibited by monoclonal antibody

A

P-type Isoamylase

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58
Q

M predominates in the normal urine

A

P-type Isoamylase

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59
Q

Migrates most quickly in terms of electrophoretic migration in AMS

A

S1 (fastest), S2, S3

P1 (follows S3), P2, P3

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60
Q

Other organs of S-type Isoamylase

A

Fallopian tube and lungs

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61
Q

Favoured by the mild alkaline conditions in the duodenum

A

P-type Isoamylase

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62
Q

The isoenzymes of salivary origin migrates most quickly (?) , P type are slower (?)

A

(S1,S2,S3)

(P1,P2,P3)

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63
Q

The most commonly observed fractions of AMS

A

P2, S1 and S2

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64
Q

In acute pancreatitis and renal failure: predominates

A

P3

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65
Q

Abnormal amylase (usually the S-type) in combination with Immunoglobulins (IgA or IgG) or other high MW proteins

A

Macroamylases

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66
Q

Not found in urine and concentrated in serum/plasma

A

Macroamylases

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67
Q

No clinical significance

A

Macroamylases

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68
Q

ELEVATIONS Prostatic isoenzyme

A
  1. Prostatic Cancerm
  2. Prostatic hyperplasia & prostatic infarction
  3. Ureteral Obstruction, carcinoid tumors of rectum & prostatic massage
  4. Medico-legal
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69
Q

: ACP is inferior to PSA

A

Prostatic Cancer

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70
Q

DECREASE Bone isoenzyme

A

• Active osteoclast-mediated bone resorption
• Gaucher’s cells
• Hairy cell leukemia

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71
Q

best marker for prostatic cancer; leading cause of death from cancer in the Ph

A

Prostate specific acntigen

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72
Q

benign condition where the prostatic gland enlargement; not cancerous

A

Prostatic hyperplasia

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73
Q

common among men aging > 60

A

Ureteral Obstruction

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74
Q

prostatic gland enlargement blocks urine flow

A

Ureteral Obstruction

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75
Q

a tumor presses the division that separates the prostate gland and the rectum

A

Carcinoid tumors of rectum

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76
Q

performed to extract a prostatic secretions

A

Prostatic massage

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77
Q

performed by stoking the prostate several times

A

Prostatic massage

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78
Q

performed in combination w/ the digital rectal exam

A

Prostatic massage

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79
Q

o px is asked to bend forward
o doctor inserts finger to the rectum until prostate gland is reached to check for enlargement

A

digital rectal exam

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80
Q

usage of bone rigidity, causing loss of important enzymes

A

Active osteoclast-mediated bone resorption

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81
Q

infiltration of the bone marrow and other tissues by Gaucher cells, which are rich in ACP activity

A

Gaucher’s cells

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82
Q

slow growing cancer of the bones

A

Hairy cell leukemia

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83
Q

affects the bone marrow making too much B lymphocytes

A

Hairy cell leukemia

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84
Q

ALP ELEVATIONS

A

• Obstructive hepatic disorder (Liver isoenzyme)
• Paget’s disease (Osteitis deformans)
• increased osteoblastic activity (Bone isoenzyme)
• DM, renal failure and cirrhosis (Intestinal isoenzyme)

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85
Q

ALP DECREASE

A

Chronic Kidney Disease patients

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86
Q

Low ALP and low Bone Turnover rate

A

ALP

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87
Q
  • bone ALP isoform in the serum of dialysis patients
A

B1x

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88
Q

 Blockage of bile ducts and pancreatic ducts

A

Obstructive hepatic disorder (obstructive jaundice)

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89
Q

 Can cause affected bones to become fragile

A

Paget’s disease

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90
Q

ALP Isoenzymes in cancer

A

Carcinoplacental Alkaline Phosphatases

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91
Q

Carcinoplacental Alkaline Phosphatases

A

Regan isoenzyme

Nagao isoenzyme

Kasahara isoenzyme

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92
Q

patients w/ a particular type of lung CA

A

Regan isoenzyme

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93
Q

Caused by ectopic production of by cancerous tissues

A

Regan isoenzyme

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94
Q

Low incidence but used in monitoring therapy

A

Regan isoenzyme

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95
Q

Adenocarcinoma of the pancreas and the bile ducts

A

Nagao isoenzyme

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96
Q

Variant of regan isoenzyme

A

Nagao isoenzyme

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97
Q

– hepatoma

A

Kasahara isoenzyme

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98
Q

GGT ELEVATIONS

A

• Liver damage
• Smoking
• Ethanol abuse
• Medication (anticonvulsant)

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99
Q

GGT DECREASE

A

• Pregnancy
• Oral contraceptives

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100
Q

GGT - major source

A

Liver damage

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101
Q
  • moderate = 10%
A

Smoking

Ethanol abuse

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102
Q
  • heavy = 20%
A

• Medication (anticonvulsant)

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103
Q

• Medication (anticonvulsant)

A

o Carbamazepine o Phenytoin o Barbiturates o Valproic acid

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104
Q

1st trimester (Cholestasis)

A

Pregnancy:

105
Q

dec. 20%

A

Oral contraceptives:

106
Q

originates primarily from the hepatobillary system

A

GGT

107
Q

may leak in the blood stream in cases of liver or bile duct damage

A

GGT

108
Q

Bile is important for digestion

A

GGT

109
Q

is the first liver enzyme to increase in the blood when any of the liver bile ducts becomes constricted

A

GGT

110
Q

is one of the most sensitive liver enzyme test for binding bile duct issues

A

GGT

111
Q

is tested alongside ALP

A

GGT

112
Q

• 2-3X ULN

A

Chronic alcoholism (heavy drinkers)

113
Q

• Affects the microsomal structure of the liver cell

A

Medication (anticonvulsant)

114
Q

• An acute type of liver problem

A

Cholestasis

115
Q

• Slower than normal flow of bile

A

Cholestasis

116
Q

• Itching, yellowing of the skin and eyes

A

Cholestasis

117
Q

GGT levels typically rise after (?), which may continue for several weeks

A

heavy alcohol intake

118
Q

2 to 6 weeks of abstinence – levels may gradually increase and come down to normal values

A

GGT

119
Q

Evaluation of liver injury: primary use

A

GGT

120
Q

The higher the level, the greater the liver damage

A

GGT

121
Q

Test for alcoholic abuse

A

GGT

122
Q

Most widely used marker for alcoholic abuse

A

GGT

123
Q

LPS ELEVATIONS

A

• perforated peptic ulcer
• duodenal ulcer
• intestinal obstruction
• mesenteric vascular obstruction

124
Q

o pancreas
o can be caused by carcinoma

A

intestinal obstruction

125
Q

NOT elevated in mumps

A

LPS

126
Q

Useful in differentiating serum amylase elevations as a result of pancreatic vs. salivary involvement

A

LPS

127
Q

In vitro reaction

A

GGT

128
Q

GGT catalyzes the transfer of (?) to the peptide group to another peptide or H2O

A

gamma-glutamyl group

129
Q

GGT transfer (?) to (?) to form (?)

A

gamma-glutamyl

glycyl-glycine

Gamma-glytamyl-glycyl-glycine

130
Q

GGT Liberation of

A

3-carboxy-4-nitroaniline

131
Q
  • most widely used substrate in GGT analysis
A

gamma-glutamyl-p-nitroanilide

132
Q

In the presence of GGT, (?) will be transferred and attach to (?) while liberating (?) forming the products, (?)

A

gamma-glutamyl

glycyl-glycine

p-nitroanilide

Gamma-glytamyl-glycyl-glycine and nitroaniline

133
Q

Stable for:
o 1 month at 4C
o 1 year at -20C

A

GGT

134
Q

-a chromogenic product w/ strong absorbance at 405-420nm

A

Nitroaniline

135
Q

Activity is stable at least 1 month at 4dc and 1 year at -20 degree Celsius

A

GGT

136
Q

GGT
is preffered but EDTA plasma has also been used

A

Non hemolyzed sample

137
Q

– produce turbidity in the reaction mixture

A

Heparin

138
Q

– depress GGT activity by 10 to 15 %

A

Citrate, oxalate and fluoride

139
Q

GGT Normal Value:

A

6-45 U/L men, 3-30 U/L women

140
Q

Responsible for starch digestion

A

AMYLASE

141
Q

Starts in the mouth with the hydrolytic action of the

A

salivary amylase

142
Q

happens in a short duration only

A

Digestion

143
Q

Upon swallowing, (?) is inactivated by the acidity of the stomach

A

amylase

144
Q

perform the majority and the rest of digestion

A

Pancreatic amylase

145
Q

Splits complex CHO made up of a-D glucose units

A

AMYLASE

146
Q

AMS TISSUE SOURCES

A

Pancrease Acinar cells
Salivary gland

147
Q

– greatest source ANS

A

Pancrease

148
Q

AMS ACTIVATORS Most effective

A

Bromide
Chloride

149
Q

Hydrolyzes glycerol esters of long chain fatty acids in the presence of H2O

A
150
Q

LPS Primary products:

A

alcohols and fatty acids

151
Q

Acts only on emulsified substrate

A

LPS

152
Q

o To force two immiscible liquids to combine into suspension
o Ex. Oil in water – will not dissolve in each other to form a uniform soln

A

LPS

153
Q

LPS TISSUE SOURCES

A
  1. Pancreas
  2. GIT
  3. Leukocytes
  4. Adipose cells
  5. Colostrum
154
Q

LPS (1° source)

A

Pancreas

155
Q

Lipase conc is about (?) greater than any organs or tissues

A

9,000x

156
Q

– first form of milk produced by the mammary glands

A

Colostrum

157
Q

Responsible for triglyceride metabolism

A

LPS

158
Q

 Bile salts
 Colipase

A

LPS

159
Q

A protein secreted by pancreas that fxs a a cofactor for pancreatic lipase, which will form a stoichiometric complex with lipase

A

Colipase

160
Q

Binds to the bile salt over triglycerol interface, thus allowing the enzymes to anchor itself to the water lipid interface to allow hydrolysis by lipase

A

Colipase

161
Q

Uses p-NPP substrate

A

Bowers and McComb Method

162
Q

• sample is serum
• plasma is rarely used

A

Bowers and McComb Method

163
Q

• Chelators falsely lower activity

A

Bowers and McComb Method

164
Q

• Enzyme activity increases slightly on storage: due to loss of inhibitors

A

Bowers and McComb Method

165
Q

• Relatively stable at 4°C up to a week

A

Bowers and McComb Method

166
Q

• Most specific method recommended by IFCC

A

Bowers and McComb Method

167
Q

• Kinetic or continuous monitoring method method (pH 10.2) which is based on the molar absorptivity of para-nitrophenol

A

Bowers and McComb Method

168
Q

• (?) (colorless cmpd) is hydrolyzed (?) (yellow) and subsequent liberation of (?)

A

p-nitrophenylphosphate

p-nitrophenol

phosphate ions

169
Q

• increase in absorbance is directly proportional to ALP activity

A

Bowers and McComb Method

170
Q

Bowers and McComb Method

SUBSTRATE
END-PRODUCTS

A

PNPP
p-nitrophenol

171
Q
  • reduces activity of intestinal & placental isoenzymes
A

Phenylalanine

172
Q
  • inhibits bone & liver isoenzymes
A

Levamisole

173
Q

measurement before and after heating

A

Heat fractionation

174
Q

identification of enzyme based on stability

A

Heat fractionation

175
Q

ALP isoenzyme
– most stable
– most labile

A

o Placental isoenzyme

o Bone isoenzyme

176
Q

Heat fractionation isoenzyme

A

o Placental isoenzyme
o Liver isoenzyme
o Bone isoenzyme

177
Q

Gutman and gutman

SUBSTRATE
END-PRODUCTS

A

Phenylphosphate
Inorganic PO4

178
Q

Shinowara

SUBSTRATE
END-PRODUCTS

A

PNPP (pnitrophenol phosphate)
p-nitrophenol

179
Q

Babson, Read and Philips

SUBSTRATE
END-PRODUCTS

A

Alpha-naphthyl PO4
Alpha-naphthol

180
Q

Roy and Hillman

SUBSTRATE
END-PRODUCTS

A

Thymolphthalein monophosphate
Free thymolphthalein

181
Q

Liberation of phosphate ions.

A

ACP

182
Q

• Reaction is measured before addition of Tartrate (Total ACP)

A

Chemical Inhibition

183
Q

• Inhibitor: Tartrate

A

Chemical Inhibition

184
Q

• After addition: Residual activity

A

Chemical Inhibition

185
Q

= Prostatic ACP

A

• Total ACP – Residual activity

186
Q

– preferred substrate for quantitative endpoint reactions (Modified by Roy)

A

• Thymolphthalein monophosphate

187
Q

• reaction is catalysed in a citrate buffer at pH 6.0

A

Prostatic ACP

188
Q

– continuous monitoring methods (Hillman method)

A

• α-naphthyl phosphate

189
Q

is the most commonly employed substrate for ACP

A

• α-naphthyl phosphate

190
Q

The primary reason for an elevated amylase is Acute pancreatitis

A

AMYLASE
LIPASE

191
Q

AMS Rise upon onset of symptoms

A

2 – 12 H
5 – 8 hours

192
Q

LPS Rise upon onset of symptoms

A

4 - 8 H
4 – 8 hours

193
Q

AMS Peak activity (fourfold to sixfold)

A

48 Hours
12 - 72 hours

194
Q

LPS Peak activity

A

4 - 8 H 4 – 8 hours

195
Q

AMS Returns to normal

A

24 Hours
24 Hours

196
Q

LPS Returns to normal

A

8 3rd – 5th day
3rd – 4th day

197
Q

The degree of elevation of AMS is helpful in differentiating diagnosis of

A

acute pancreatitis

198
Q

AMS Other conditions

A
  1. Mumps
  2. Perforated peptic ulcer
  3. Appendicitis
  4. Ruptured ectopic pregnancy
  5. Dissecting aortic aneurysm
  6. Biliary tract disease
199
Q

– caused by a virus; young adults/children experience fever, muscle pain, headache, poor appetite, tiredness followed by painful swelling of one or both carotid salivary glands

A

Mumps

200
Q

AMS Most popular method

A

Continuous Monitoring Method

201
Q

Improved the reaction stoichiometry (quantitative study of reactants and products in a chem rx)

A

Continuous Monitoring Method

202
Q

more controlled and consistent hydrolysis conditions

A

Continuous Monitoring Method

203
Q

makes use of coupling of several enzyme systems to monitor amylase activity

A

Continuous Monitoring Method

204
Q

AMS Substrates: Small oligosaccharides

A

 Maltopentose  Maltopentrose  4-NP-glcoside

205
Q

AMS Historical methods

A
206
Q

Uses starch substrate hydrolyzed to carbohydrate molecule w/ reducing properties

A

Saccharogenic

207
Q

The amount of reducing sugars are then measured where the concentration is directly proportional to AMS activity

A

Saccharogenic

208
Q

Classic reference method for amylase activity

A

Saccharogenic

209
Q

Units: Somogyi

A

Saccharogenic

210
Q

Hydrolysis of starch by amylase causes a decrease in color intensity

A

Amyloclastic (Iodometric method)

211
Q

Starch substrate-attached to iodine, AMS hydrolyze starch and iodine is released-decrease in the intensity of the initial dark blue complex-the decrease is proportional to AMS conc.

A

Amyloclastic (Iodometric method)

212
Q

Measures the disappearance of starch substrate

A

Amyloclastic (Iodometric method)

213
Q

Use a starch substrate to which a chromogenic dye has been attached, forming an insoluble dye–substrate complex.

A

Chromogenic (Klein, Foreman, Searcy)

214
Q

Opposite to amyloclastic

A

Chromogenic (Klein, Foreman, Searcy)

215
Q

The increase in color intensity of soluble dye-substrate solution is proportional to AMS activity, measure increase in color from production of product couples with a chromogenic dye

A

Chromogenic (Klein, Foreman, Searcy)

216
Q

Measures the change in turbidity of starch solution over a short reaction period

A

Turbidimetry and Nephelometry (Peralta & Reinhart)

217
Q

Grouped depending of what substrate is used in a particular method

A

LPS

218
Q

LPS Specimen

A

serum (stable at RT), pleural fluid, ascitic fluid

219
Q

LPS Inhibitors

A

heavy metals, quinine & some esterase inhibitors

220
Q

increases concentration of LPS

A

Bacterium

221
Q

Some important lipase-producing bacterial genera include

A

Bacillus, Pseudomonas and Burkholderia

222
Q

LPS Not inhibited by

A

fluoride or arsenilate

223
Q

Most important dietary lipids. Digestion depends on the interplay among pancreatic lipase, colipase, and bile acids/salts.

A

For Long-Chain Triglycerol Substrate

224
Q

– hydrolyses these triglycerides into fatty acid molecules and mono-acyl glycerols

A

Pancreatic lipase

225
Q

fatty acid is titrated w/ alkali solution

A

Titrimetric Methods

226
Q

Titrimetric Methods

A
227
Q

titration is carried out by potentiometry

A

pH meter (potentiometric titration)

228
Q

procedure to determine the conc of a given analyte

A

pH meter (potentiometric titration)

229
Q

used to characterize acids

A

pH meter (potentiometric titration)

230
Q

no chemical indicator

A

pH meter (potentiometric titration)

231
Q

electric potential across substance is being measured

A

pH meter (potentiometric titration)

232
Q

Turbidimetric Methods

A
233
Q

emulsion of fats produces milky appearance

A

Turbidimetric Methods

234
Q

simpler or more rapid method

A

Turbidimetric Methods

235
Q

fats in the soln creates a cloudy emulsion

A

Turbidimetric Methods

236
Q

as the fats are hydrolysed by lipase, the particles will disperse

A

Turbidimetric Methods

237
Q

measures the rate of dispersing or clearing, which will give an estimation of lipase activity

A

Turbidimetric Methods

238
Q

: fatty acids are extracted using Petroleum ether

A

Myrtle and Zell method

239
Q

Fatty acid + chemical reagent:

A

Fluorescein (4methyl bellifuzone)

240
Q

For Short-Chain TG Substrate Examples

A

Acetate, Prothionate, Butyrate, TG produced by bacteria in the gut during fermentation, manmade substrates

241
Q

For Short-Chain TG Substrate
Advantages

A

Analytical, greater solubility in aqueous medium

242
Q

For Short-Chain TG Substrate
Disadvantage

A

unphysiologic substrate

243
Q

– Tributyrin

A

Erlanson & Bergstrom

244
Q

makes use of 1251-labeled lipase

A

Radioimmunoassay

245
Q

antibodies to pancreatic lipase are bound to latex particles

A

Latex Agglutination

246
Q

Gutman and gutman

A

Phenylphosphate
Inorganic PO4

247
Q

Shinowara

A

PNPP (pnitrophenol phosphate)
p-nitrophenol

248
Q

Babson, Read and Philips

A

Alpha-naphthyl PO4
Alpha-naphthol

249
Q

Roy and Hillman

A

Thymolphthalein monophosphate
Free thymolphthalein

250
Q

Liberation of phosphate ions.

A

ACP

251
Q

Reaction is measured before addition of Tartrate (Total ACP)

A

Chemical Inhibition

252
Q

Chemical Inhibition
Inhibitor:

A

Tartrate

253
Q

After addition: Residual activity

A

Chemical Inhibition

254
Q

= Prostatic ACP

A

Total ACP – Residual activity

255
Q

– preferred substrate for quantitative endpoint reactions (Modified by Roy)

A

Thymolphthalein monophosphate

256
Q

reaction is catalysed in a citrate buffer at pH 6.0

A

Prostatic ACP

257
Q

– continuous monitoring methods (Hillman method)

A

α-naphthyl phosphate

258
Q

is the most commonly employed substrate for ACP

A

α-naphthyl phosphate

CC2 LECTURE (33 decks)

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