Advances in Comparative Physiology and Biochemistry by O. Lowenstein

By O. Lowenstein

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I. Rajasingham et al. (1971) Rajasingham et al. I. I. I. Ettalibi et al. (1975) Hesselholt et al. 1966); Rajasingham et al. I. I. S. I. = Starch-iodine assay. Characteristics of α-glucosidase rather t h a n α-amylase (see text). 20), a common lysosomal acid hydrolase which is an exoamylase. y 1976). If these criteria have been applied to the Tetrahymena enzyme(s), the results have not been reported. Identification of apparent starch-degrading activity by using the starch-iodine reaction has been criticized from several standpoints, particularly the observation t h a t spurious activity is obtained in the presence of proteins such as albumin (see Section ΙΙ,Β).

Each of the isozymes remained homogenous during purification steps and tryptic digests of each isozyme contained some unique spots. Although the authors discussed limited proteolysis as a potential source of the different rabbit isozymes, they felt the data were more supportive of multiple genes, each coding for one of the iso­ zymes. Berk and his colleagues (1963) performed paper electrophoresis 48 ROBERT C. KARN AND GEORGE M. MALACINSKI la Ic lb 2a 2b ( 2c • 3o 3b 3c FIG. 16. 1. The amylase isozymes are la­ beled Aj through A4 beginning with the band closest to the origin.

When two isozymes are present, they vary quantitatively, apparently in a genetically determined fashion (see Section VI). Pancreatic phenotypes, on the other hand, consist of two isozymes with slower electrophoretic mobilities t h a n those of sa­ liva. Nielsen (1969) reported finding no pancreatic variants in 80 speci­ mens. The serum amylase pattern differed from both the salivary and 46 ROBERT C. KARN AND GEORGE M. MALACINSKI pancreatic patterns, having only one isozyme in common with saliva and none in common with the pancreas.

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