Evaluation of Analytical Techniques for Quantification of Poultry α-Amylase

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.

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The amylase gene-enzyme system of chickens. II. Biochemical characterization of allozymes

Gapusan

Yardley

Hughes

1990

Biochem Genet

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Effect of Decreased Feed Intake on Serum and Pancreatic α-Amylase of Broiler Chickens

Rodeheaver¹,

Wyatt²

1984

Avian Diseases

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Removal of feed from 20-day-old broiler chicks for 24 hours caused serum and pancreatic alpha-amylase activities to increase almost twofold. A 24-hour feeding period following feed removal caused a reduction in serum alpha-amylase to basal levels and a sixfold reduction in pancreatic alpha-amylase activity. Serum alpha-amylase levels remained elevated after long-term feed restriction in adult broilers compared with levels in full-fed controls. Reduction in feed intake in chicks caused by coccidial infections also resulted in increased serum alpha-amylase. In all cases, the degree of change in serum alpha-amylase corresponded inversely to feed intake. It is proposed that the pancreas synthesizes a specific quantity of alpha-amylase, which does not change even under conditions of extended underconsumption of feed. The rate of alpha-amylase secretion is determined, at least indirectly, by the rate of carbohydrate metabolism, and the remainder of the enzyme is stored in the pancreatic cells. A small percentage of the stored enzyme diffuses into the blood and thus directly reflects increased secretion or accumulation of alpha-amylase in the pancreas in response to conditions of carbohydrate utilization.

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Distribution of α-Amylase Activity in Selected Broiler Tissues

Rodeheaver

Wyatt

1986

Poultry Science

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In an examination of broiler alpha-amylase, significant variation in the serum enzyme activity level was noted, adult levels were lower than those of young chicks. Analysis of alpha-amylase activity in various body fluids and tissues of 11-day and 7-week-old broilers indicated that the liver cannot be considered a source of alpha-amylase, although there was activity in both liver tissue and bile of 10 units/g wet weight and 35 units/100 ml, respectively. Fluid from the oral cavity had low levels of alpha-amylase activity, less than 100 units/100 ml, which decreased with age, indicating that the salivary glands may synthesize some alpha-amylase but are not a primary source. Sonication of the pancreatic homogenates was found to significantly increase the apparent activity of alpha-amylase 35-fold over unsonicated homogenates. The pancreas was the major source of alpha-amylase with activities ranging from 89 X 10(2) to 445 X 10(2) units/g wet weight. The level of activity increased with age of the bird. The electrophoretic zymograms of serum, liver, and pancreatic homogenates indicate a similar pancreatic origin for the alpha-amylase found in each tissue or fluid.

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Evaluation of Analytical Techniques for Quantification of Poultry α-Amylase

Cited by 3 publications

References 23 publications

The amylase gene-enzyme system of chickens. II. Biochemical characterization of allozymes

The amylase gene-enzyme system of chickens. II. Biochemical characterization of allozymes

Effect of Decreased Feed Intake on Serum and Pancreatic α-Amylase of Broiler Chickens

Distribution of α-Amylase Activity in Selected Broiler Tissues

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