Advances in Comparative Physiology and Biochemistry - download pdf or read online

By O. Lowenstein

ISBN-10: 0120115077

ISBN-13: 9780120115075

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The source of serum amylase has not been identified in many animal species tested. Confirmation of the source of the serum amylase isozyme(s) can be obtained by observing genetic variation corresponding to that observed in a particular tissue source. Such an observation led Hope and Finnegan (1970) to attribute the genetically variable amylase isozyme in the serum of the brushtailed possum to the pancreas. A second series of isozymes appeared to be of salivary origin, although no variants were ascertained.

Furthermore, the major iso­ zymes were shown to differ isoelectrically (Fig. 16, 3a-c) and to shift to more anodal forms when incubated at elevated pH. The authors compared their observations with those of Kauffman et al. (1970) on human amylase and concluded that some of the isozymes might be the result of posttranslational modifications, such as deamidation (of glutamine and/or asparagine residues). , 1973), no carbohydrate studies of rat sali­ vary amylase are available. Similarly, the more negatively charged major isozyme of rat pancreatic amylase (Sanders and Rutter, 1972) may result from deamidation of the less negatively charged major iso­ zyme, but observations of isozyme conversion have not yet been re­ ported.

1975b). , 1975b). The data given in Figs. 8 and 9 have been cited as evidence t h a t modified amylase is still partially active. TheKm of the modified enzyme (Fig. 9) is identical to native enzyme, suggesting t h a t the substrate binding site of the enzyme does not require -SH groups for activity. A number of amino acids have been implicated to be functional groups necessary for the activity of the enzyme. The literature on this aspect of amylase chemistry, which goes back over 35 years to a report by Little and Caldwell (1942), remains in many cases contradictory, and in still other cases conjectural.

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Advances in Comparative Physiology and Biochemistry by O. Lowenstein


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