The amylase gene-enzyme system of chickens. II. Biochemical characterization of allozymes.
The chicken amylase allozymes, AmyF and AmyS, were extracted from pancreatic tissues of AmyF/F and AmyS/S individuals and purified. Activities were measured under various reaction conditions (= treatments) to assess whether the allozymes were functionally different. The amylases had properties typical of alpha-amylases, i.e., both were inhibited by ethylenediaminetetraacetate and alpha-amylase inhibitor from wheat, had pH optima between 7.0 and 8.0, and could utilize a variety of substrates containing alpha 1,4 linkages. The amylases were also found to be inhibited by potassium phosphate buffer and p-chloromercuribenzoate. In terms of substrate specificity, both amylases could utilize all of the substrates tested with activity observed in the following order: amylopectin greater than potato starch greater than dextrin greater than glycogen greater than amylose. Statistical analysis indicated significant functional differences between the two allozymes in terms of specific activities, substrate specificities, and inhibitor sensitivities. AmyF had a significantly lower specific activity than did AmyS. The amylases responded differently to the substrate amylose, with AmyF better able to digest this substrate. AmyS was less sensitive than AmyF to alpha-amylase inhibitor from wheat.
Gapusan
R A
RA
Department of Biological Sciences, Clemson University, South Carolina 29634-1903.
Yardley
D G
DG
Hughes
B L
BL
D000681:Amylases / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D002645:Chickens / Q000235:genetics; D002729:Chloromercuribenzoates / Q000494:pharmacology; D007527:Isoenzymes / Q000235:genetics / Q000378:metabolism; D007700:Kinetics; D010179:Pancreas / Q000201:enzymology; D011110:Polymorphism, Genetic; D013379:Substrate Specificity
D002729:Chloromercuribenzoates; D007527:Isoenzymes; D000681:Amylases