Determination of alpha-amylase activity in dextran, ficoll and polyethylene glycol solutions

1992 ◽  
Vol 6 (2) ◽  
pp. 177-180
Author(s):  
Ivo Šafařík ◽  
Miroslava Šafaříková
Keyword(s):  
Polyethylene Glycol ◽  
Amylase Activity ◽  
Alpha Amylase

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.

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.

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

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.

Rapid determination of alpha-amylase activity by use of a new chromogenic substrate.

1987 ◽  
Vol 33 (4) ◽  
pp. 524-528 ◽  
Author(s):  
G Dupuy ◽  
G Hilaire ◽  
C Aubry
Keyword(s):  
Amylase Activity ◽  
Rapid Determination ◽  
Molar Absorptivity ◽  
Cleavage Product ◽  
Alpha Amylase ◽  
Lag Phase ◽  
Chromogenic Substrate ◽  
Salivary Alpha Amylase ◽  
Alpha Glucosidase

Abstract A new chromogenic substrate that is blocked at the nonreducing end, 4,6-benzylidene-alpha-D-4-nitrophenylmaltoheptaoside, is used to determine alpha-amylase (EC 3.2.1.1) activity in serum in a coupled assay with alpha-glucosidase (EC 3.2.1.20) and glucoamylase (EC 3.2.1.3) as auxiliary enzymes. The duration of the lag phase between 25 and 37 degrees C is less than 90 s, and the molar absorptivity of 4-nitrophenol is constant. The main cleavage product of the substrate by human pancreatic and salivary alpha-amylase is 4-nitrophenylmaltoside; in the presence of the auxiliary enzymes, greater than 95% of hydrolyzed substrate is accounted for as 4-nitrophenol. The combined reagent is stable for at least 20 days at 2-8 degrees C; precision is good, with CVs ranging from 1.7 to 3.3%; and the correlation of results with those by the 4-nitrophenylmaltoheptaoside method is excellent. Heparin (40 kilo-int. units/L), ascorbic acid (2.8 mmol/L), bilirubin (430 mumol/L), hemoglobin (170 mumol/L), glucose (55 mmol/L), and triglycerides (11 mmol/L) do not interfere in the assay.

scholarly journals Genetic Study of Pre-Harvest Sporouting Tolerance in Winter Wheat

2011 ◽  
Vol 68 (1) ◽  
Author(s):  
Nicolae LUPU ◽  
Vasile MOLDOVAN ◽  
Rozalia KADAR ◽  
Ioan HAS ◽  
Ionuţ RACZ
Keyword(s):  
Winter Wheat ◽  
Genetic Study ◽  
Quantitative Trait ◽  
Amylase Activity ◽  
Alpha Amylase ◽  
F1 Hybrids ◽  
Falling Number ◽  
Gene Effects ◽  
Physiological Characters

Pre-harvest sprouting process in winter wheat can be considered as a complex quantitative trait because it is the result of some morpho-physiological characters among dormancy duration and alpha-amylase activity, are essential. The objectives of this study consist of two main aspects:evaluation of dormancy duration in F1 hybrids in comparison to parents. determination of gene effects involved in inheritance of pre-harvest sprouting and falling number in winter wheat.

Sign in / Sign up

Export Citation Format

Share Document