By O. Lowenstein

ISBN-10: 0120115077

ISBN-13: 9780120115075

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They ruled out subunit cross association as an explanation of their isozyme patterns. Robinovitch and Sreebny (1972) performed a detailed electrophoretic study of purified rat parotid amylase, conclud­ ing that there were three major (Ag-AJ and one minor (AJ isozymes distinguishable in anionic polyacrylamide gel electrophoresis (Fig. 16). Preparative polyacrylamide gel electrophoresis revealed isozyme A2 to be the dominant species. Subsequent molecular weight determina­ tions, using SDS electrophoresis, demonstrated isozyme Aj to have a higher molecular weight (62,400) than the major isozymes (A2-A4), all of which had a molecular weight of 56,700.

A second series of isozymes appeared to be of salivary origin, although no variants were ascertained. 44 ROBERT C. KARN AND GEORGE M. ■! SERUM PANCREAS SERUM PANCREAS RABBIT: PANCREAS ■1 OORUB PANCREAS HORSE' 0 1 Q 1 0 D NKMlt FIG. 14. Amylase isoenzyme patterns of extracts of human and other mammalian tis­ sues on polyacrylamide gel electrophoresis. (Reproduced from Rajasingham, 1971. Enzyme 12, 180-186. Reprinted by permission of S. ) Finnegan and Hope (1970) also observed genetic variants of pancre­ atic amylase reflected in the serum of the marsupial mouse but could find no amylase in the saliva or in extracts of heart, liver, kidney, and intestine.

Nonetheless, it is apparent that the Ami gene products differ from classic α-amylases and care should be taken in comparing electrophoretic data from studies of ani­ mal sera. Human amylase isozyme patterns are perhaps the best understood of animal amylases studied to date. The human α-amylases have recently been reviewed by Merritt and Karn (1977). The isozyme phenotypes will be described in summary here. , 1971). Kauffman et al. (1970) showed that purified salivary amylase could be separated into two components on Biogel P-100 chromatography and that each com­ ponent consisted of a series of isozymes on electrophoresis.

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Advances in Comparative Physiology and Biochemistry by O. Lowenstein

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