Advances in Comparative Physiology and Biochemistry by O. Lowenstein

By O. Lowenstein

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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. 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.

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. Perhaps the most confusing rate amylase isozyme patterns have been obtained from serum and from liver extracts. Hammerton and Messer (1971) showed that rat serum amylase migrated similarly to rat liver amylase on cellulose acetate electrophoresis, a finding in agreement with the suggestion by Arnold and Rutter (1963) that the ANIMAL α-AMYLASES 47 liver was the major, if not the only, source of serum amylase.

Keller et al. (1971) showed that the covalently bound carbohydrate ofthat en­ zyme includes glucosamine, galactose, mannose, and fucose but not sialic acid. , 1971) and tryptic peptides (Watanabe and Keller, 1974) revealed that the carbohydrate was covalently bound to the protein as at least two separate moieties. More recently, Mayo and Carlson (1974) purified human submandibular amylase and reported that it contains sialic acid as well as the sugars Keller had reported for human parotid amy­ lase.

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