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.
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This study was supported in part by the FEISDED program and is Technical Contribution Number 3120 of the South Carolina Agricultural Experimental Station, Clemson University.
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Gapusan, R.A., Yardley, D.G. & Hughes, B.L. The amylase gene-enzyme system of chickens. II. Biochemical characterization of allozymes. Biochem Genet 28, 553–560 (1990). https://doi.org/10.1007/BF00553947
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DOI: https://doi.org/10.1007/BF00553947