ISSN:
1573-4927
Keywords:
amylase
;
allozyme
;
polymorphism
;
functional properties
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
Abstract The chicken amylase allozymes, AmyF and AmyS, were extracted from pancreatic tissues ofAmy F/FandAmy S/Sindividuals and purified. Activities were measured under various reaction conditions (=treatments) to assess whether the allozymes were functionally different. The amylases had properties typical of α-amylases, i.e., both were inhibited by ethylenediaminetetraacetate and α-amylase inhibitor from wheat, hadpH optima between 7.0 and 8.0, and could utilize a variety of substrates containing α 1,4 linkages. The amylases were also found to be inhibited by potassium phosphate buffer andp-chloromercuribenzoate. In terms of substrate specificity, both amylases could utilize all of the substrates tested with activity observed in the following order: amylopectin 〉 potato starch 〉 dextrin 〉 glycogen 〉 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 α-amylase inhibitor from wheat.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00553947
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