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

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Abstract

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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Authors and Affiliations

  1. Department of Medical Genetics, Indiana University Medical Center, Indianapolis, Indiana

    R. C. Karn, Jeff D. Shulkin, A. Donald Merritt & Ruth C. Newell

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  1. R. C. Karn
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  2. Jeff D. Shulkin
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  3. A. Donald Merritt
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  4. Ruth C. Newell
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Additional information

This investigation was supported in part by PHS Research Grant GM-19178.

Supported by PHS Training Grant DE 119.

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Karn, R.C., Shulkin, J.D., Merritt, A.D. et al. Evidence for post-transcriptional modification of human salivary amylase (Amy1) isozymes. Biochem Genet 10, 341–350 (1973). https://doi.org/10.1007/BF00485989

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  • DOI: https://doi.org/10.1007/BF00485989

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