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Evidence for post-transcriptional modification of human salivary amylase (Amy1) isozymes

✍ Scribed by R. C. Karn; Jeff D. Shulkin; A. Donald Merritt; Ruth C. Newell

Publisher: Springer
Year: 1973
Tongue: English
Weight: 513 KB
Volume: 10
Category: Article
ISSN: 0006-2928
DOI: 10.1007/bf00485989

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✦ Synopsis

Human parotid salivary amylase (Amy1) isozymes may be separated into two families: (1) one of higher molecular weight and slower electrophoretic mobility, odds, and ( 2) the other of lower molecular weight and faster electrophoretic mobility, evens. An enzyme has been detected in whole saliva, and also partially purified from human oral bacterial flora, which converts the isoamylases from odds to evens. No similar modifying activity was detected in parotid saliva or submandibular and sublingual salivas. A model is presented which explains the multiple isozymes of salivary amylase by post-transcriptional modification of a single gene product.

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