scholarly journals Antenatal development of amylase isoenzymes.

1972 ◽  
Vol 9 (3) ◽  
pp. 321-323 ◽  
Author(s):  
R Laxova
Keyword(s):  
Antenatal Development ◽  
Amylase Isoenzymes

Quantitative gel-electrophoretic determination of serum amylase isoenzyme distributions.

1979 ◽  
Vol 25 (11) ◽  
pp. 1919-1923 ◽  
Author(s):  
B K Gillard
Keyword(s):  
Differential Diagnosis ◽  
Disease Progression ◽  
Quantitative Method ◽  
Serum Amylase ◽  
Soluble Starch ◽  
Normal Serum ◽  
Polyacrylamide Gel ◽  
Starch Solution ◽  
Amylase Isoenzymes

Abstract I report a direct, sensitive, quantitative method for determining serum amylase isoenzyme activity with commercially available reagents. Day-to-day reproducibility (CV) was 3--4% for the isoenzymes in normal serum; within-run precision was 8, 3, and 2% for low, normal and high isoenzyme activities. Amylase isoenzymes, separated into the pancreatic and salivary types by electrophoresis in polyacrylamide gel, are then quantified by directly incubating the gels in soluble-starch solution, staining with iodine, and densitometry. The proportion of pancreatic isoenzyme (47 normal sera) was 43 +/- 8% (mean +/- SD). Isoenzyme activities as low as 2% of normal can be measured accurately in 10 micro L of serum. The reproducibility, precision, and sensitivity indicate that the method is applicable to differential diagnosis of hyperamylasemia or hypoamylasemia, and is suited for monitoring the subtle changes in serum amylase isoenzyme distribution that may accompany disease progression or therapy.

Identification of amylase isoenzymes in intestinal contents

1984 ◽  
Vol 29 (4) ◽  
pp. 297-299 ◽  
Author(s):  
Peter A. Banks ◽  
Andrew L. Warshaw ◽  
Gail Z. Wolfe ◽  
Alexandra Engalichev ◽  
Denise Duchainey
Keyword(s):  
Intestinal Contents ◽  
Amylase Isoenzymes

Methods compared for determining total amylase activity and amylase isoenzymes in serum.

1989 ◽  
Vol 35 (4) ◽  
pp. 645-648 ◽  
Author(s):  
J L Badenoch ◽  
R Bals
Keyword(s):  
Monoclonal Antibody ◽  
Amylase Activity ◽  
Reference Interval ◽  
Total Activity ◽  
Alpha Amylase ◽  
Excellent Correlation ◽  
Kinetic Methods ◽  
Antibody Method ◽  
Isoenzyme Composition ◽  
Amylase Isoenzymes

Abstract We evaluated two kinetic methods for determining total amylase activity and isoenzyme composition in serum. Stability studies of reagents for measuring total activity indicate that reagents containing 4-nitrophenyl-alpha-glucosides or enzyme-linked reagents can be stored only for seven days at 4 degrees C. Methods based on 4-nitrophenyl-alpha-glucoside substrates cannot be used if the reagent absorbance at 405 nm exceeds 2. However, in the alpha-amylase EPS method (Boehringer Mannheim) an ethylidene-protected 4-nitrophenyl-alpha-D-maltoheptaoside substrate is stable for up to 28 days after reconstitution. Further studies indicated that the Amylase-DS (Beckman) and the alpha-Amylase EPS standard curves are linear to at least six times the upper limit of the reference interval. Within-batch imprecision (CV less than 1.1%) and between-batch imprecision (CV less than 3.3%) for these two methods are comparable with those for other kinetic methods, and there is excellent correlation (r2 = 0.983) between the two methods. The reference interval, determined by use of samples from 90 healthy blood donors, is 31 to 141 U/L for the amylase-DS method, 22 to 92 U/L for the alpha-Amylase EPS method. We also used these two methods to measure amylase isoenzymes after inhibiting the salivary isoenzyme with either a lectin or a monoclonal antibody. We found the monoclonal antibody method more specific than the lectin inhibition method for determining the isoenzymes.

Specific immunoassay of alpha-amylase isoenzymes in human serum.

1985 ◽  
Vol 31 (8) ◽  
pp. 1331-1334 ◽  
Author(s):  
M Gerber ◽  
K Naujoks ◽  
H Lenz ◽  
W Gerhardt ◽  
K Wulff
Keyword(s):  
Monoclonal Antibody ◽  
Human Serum ◽  
Enzyme Immunoassay ◽  
Amylase Activity ◽  
Alpha Amylase ◽  
Pancreatic Amylase ◽  
Routine Method ◽  
Salivary Amylase ◽  
Amylase Isoenzymes

Abstract A monoclonal antibody (66C7) was prepared that specifically binds human salivary amylase (EC 3.2.1.1); it cross reacts with human pancreatic amylase by less than 1%. Two procedures are described for determination of isoamylases in human serum with this antibody: an enzyme immunoassay for determining amylase of salivary origin, and a routine method in which this amylase is immunoprecipitated and the remaining (pancreatic) amylase activity is assayed. Results by the two methods correlate well.

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