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By O. Lowenstein

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1970) demonstrated that a portion of human parotid salivary amylase was glycosylated. 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.

1975b) but so far no evidence of this type is available. Malacinski and Rutter (1969) have performed the only intensive study of rabbit amylases to date. They demonstrated a single isozyme from the parotid gland which differed from the three isozymes they ob­ tained from the pancreas. 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.

They also observed minor forms of the pancreatic enzyme as well as one major and one minor form of salivary amylase using analytical gel isoelectric focusing. Their analyses of the major forms of pancreatic and parotid amylases led them to conclude that the native enzymes were single polypeptide chains. 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.

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