Suitability of control materials for determination of alpha-amylase activity.

1981 ◽  
Vol 27 (6) ◽  
pp. 806-815 ◽  
Author(s):  
J P Bretaudiere ◽  
R Rej ◽  
P Drake ◽  
A Vassault ◽  
M Bailly
Keyword(s):  
Quality Control ◽  
Human Serum ◽  
Amylase Activity ◽  
Linear Representation ◽  
Alpha Amylase ◽  
Reference Groups ◽  
The Matrix ◽  
Components Analysis ◽  
Pancreatic Pathology

Abstract The suitability of control materials for determination of alpha-amylase activity was assessed in comparison with reference groups of authentic human serum specimens containing alpha-amylase of either pancreatic or salivary origin, specimens from patients with no pancreatic pathology, and normal specimens to which porcine pancreatic alpha-amylase was added. After determination of alpha-amylase activity by 11 commonly used techniques (five different principles), the results were processed by both classical (linear representation, regression) and multivariate (correspondence analysis, principal-components analysis) statistical techniques. Specimens containing porcine pancreatic alpha-amylase did not behave like any of the other groups. We conclude that porcine enzyme should not be used for interlaboratory quality-control surveys or intermethod comparison studies. Determination of human salivary and pancreatic alpha-amylase showed intermethod biases similar to those for authentic patients' specimens. Human salivary alpha-amylase, both because of its behavior and its commercial availability, is a satisfactory source for alpha-amylase activity of quality-control specimens. The nature of the matrix (polyvinylpyrrolidone, albumin, delipidated serum, bovine serum, or human serum) little influenced the behavior of the specimens for any of the methods studied.

Determination of alpha-amylase activity: methods comparison and commutability study of several control materials

1995 ◽  
Vol 41 (3) ◽  
pp. 435-438 ◽  
Author(s):  
G Gubern ◽  
F Canalias ◽  
F J Gella
Keyword(s):  
Human Serum ◽  
Amylase Activity ◽  
Alpha Amylase ◽  
Human Origin ◽  
Serum Samples ◽  
Chromophore Group ◽  
Laboratory Control ◽  
Wide Range ◽  
Human Sera

Abstract Six different methods for alpha-amylase determination were compared by assaying human serum samples covering a wide range of alpha-amylase values. All the methods studied use as substrate a maltooligosaccharide with a chromophore group at the reducing end; some are chemically blocked at the nonreducing end. Intermethod comparison by regression and correspondence analyses showed significant differences for two methods. The commutability of 12 commercial control materials containing alpha-amylase was also assessed by the different methods in comparison with human serum specimens containing the pancreatic and salivary isoenzymes. We also studied the behavior of pancreatic and salivary materials prepared in our laboratory. Control materials with alpha-amylase of non-human origin were not commutable with the enzyme in human sera and should not be used for intermethod calibration.

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.

New saccharogenic determination of alpha-amylase in serum and urine.

1979 ◽  
Vol 25 (2) ◽  
pp. 215-217 ◽  
Author(s):  
L van Leeuwen
Keyword(s):  
Human Serum ◽  
Amylase Activity ◽  
Glucose Dehydrogenase ◽  
Alpha Amylase ◽  
Endogenous Glucose ◽  
Alpha Glucosidase ◽  
Serum And Urine

Abstract I describe a new kinetic enzymatic saccharogenic method for assaying alpha-amylase in human serum and urine. alpha-Amylase liberates maltose from starch. This is successively acted on by alpha-glucosidase, mutarotase, and glucose dehydrogenase. The resulting conversion of NAD+ to NADH, measured at 340 nm, during a 20-min incubation reflects amylase activity. Endogenous glucose is destroyed before measurement of amylase activity is begun.

Enzyme-coupled ultraviolet determination of alpha-amylase activity with the GEMSAEC centrifugal analyzer.

1978 ◽  
Vol 24 (9) ◽  
pp. 1620-1624 ◽  
Author(s):  
W H Porter ◽  
R E Roberts
Keyword(s):  
Linear Response ◽  
Amylase Activity ◽  
Kinetic Studies ◽  
Alpha Amylase ◽  
Coefficients Of Variation ◽  
Endogenous Glucose ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Alpha Glucosidase ◽  
As Effects

Abstract We evaluated the Harleco alpha-glucosidase/hexokinase/glucose-6-phosphate dehydrogenase-coupled alpha-amylase method, bu use of the GEMSAEC centrifugal analyzer. Performance evaluation included kinetic studies of substrate and maltose hydrolysis as well as effects of endogenous glucose and fructose. The reagent was found to give a linear response with alpha-amylase activity to greater than 1200 U/liter. Within-run precision resulted in coefficients of variation (CV) of 0.9 to 3.2% over the range studied. Day-to-day precision corresponded to CV's of 2.4 to 4.4% over the same range of alpha-amylase procedure was found to be good (r = 0.997) for patients' sera examined.

Inhibition of Human Serum Alpha-Amylase Activity

Enzyme ◽  
1983 ◽  
Vol 30 (1) ◽  
pp. 66-69
Author(s):  
K. A. (a) Sobiech ◽  
A. (b) Gladysz ◽  
J. (b) Molin
Keyword(s):  
Human Serum ◽  
Amylase Activity ◽  
Alpha Amylase

Isopropylidine maltoheptosyl fructofuranoside, doubly blocked substrate for determination of endoamylase activity

1991 ◽  
Vol 37 (8) ◽  
pp. 1323-1328
Author(s):  
Z Ogawa ◽  
Y Matsubayashi ◽  
S Satoh ◽  
N Orita ◽  
H Itoh
Keyword(s):  
Human Serum ◽  
Coefficient Of Variation ◽  
Oxidation Rate ◽  
Amylase Activity ◽  
Mannitol Dehydrogenase ◽  
Coupled Reactions ◽  
Alpha Glucosidase ◽  
Serum And Urine

Abstract We synthesized o-(4,6-o-isopropylidene-alpha-D-glucopyranosyl)-(1----4)- [o-alpha-D-glucopyranosyl-(1----4])5-o-alpha-D-glucopyranosyl-(1----2)- alpha-D-fructofuranoside (IPG7F) and developed an assay for determining the activity of amylase in human serum and urine by using this substrate. Glucoamylase, alpha-glucosidase, and mannitol dehydrogenase are used as coupling enzymes. The coupled reactions are monitored by continuously measuring the oxidation rate of NADH. In this procedure, various substances in the test specimens do not interfere with the detection of amylase activity. Exactly one molecule of NADH is oxidized by one attack of amylase on the substrate, although four products can be produced in the reaction. The within-assay coefficient of variation (CV) ranged from 1.0% to 4.1% and the between-assay CV ranged from 2.6% to 5.3%. The results of our new assay correlate well with those of the amylase assay involving p-nitrophenol maltoheptaoside as substrate (r = 0.978) and with those of the amylase assay involving maltopentaose (r = 0.987).

Determination of Phenolics and Antioxidant Properties in Tea and the Effects of Polyphenols on Alpha-Amylase Activity

2015 ◽  
Vol 14 (11) ◽  
pp. 808-817 ◽  
Author(s):  
N.I. Nadiah ◽  
L.H. Cheng ◽  
M.E. Azhar ◽  
A.A. Karim ◽  
U. Uthumporn ◽  
...  
Keyword(s):  
Amylase Activity ◽  
Antioxidant Properties ◽  
Alpha Amylase
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