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.

The amylase gene-enzyme system of chickens. I. Allozymic and activity variation.

Amylase allozymic and activity variation was studied in three flocks of chickens (Gallus domesticus). Individuals from one flock were studied to assess the effects of sex, tissue, and genotype on amylase activity. Additionally, the allozymes were purified and their specific activities compared. Variation was observed within and among the flocks. Two alleles were found to be segregating in the flocks, one flock being polymorphic and the other two monomorphic. Mean amylase activities among the three flocks were significantly different. The relationship of this activity variation to regulatory variation is discussed. There were no significant effects of sex or genotype on amylase activity and, in most cases, no correlation between activities in the various tissues. However, in heterozygotes one of the alloamylases had much lower activity than the other.