Immunological relationships and post-translational modifications of human salivary amylase (Amy1) and pancreatic amylase (Amy2) isozymes |
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| Authors: | R. C. Karn Barnett B. Rosenblum Jewell C. Ward A. Donald Merritt Jeff D. Shulkin |
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| Affiliation: | (1) Department of Medical Genetics, Indiana University Medical Center, Indianapolis, Indiana;(2) Division of Medical Genetics, Harbor General Hospital Campus, UCLA School of Medicine, Torrance, California |
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| Abstract: | Electrophoretic phenotypes of human salivary amylase (Amy1) and pancreatic amylase (Amy2) consist of complex isozyme patterns which may result from post-translational modifications of the primary products of the amylase loci. Biochemical separation of the two molecular weight families of salivary amylase and development of a new electrophoretic system have allowed the identification of complete isozyme patterns corresponding to variant alleles in Amy1 and Amy2 heterozygotes. Further, immunological studies show no nonidentities among salivary isozymes and among pancreatic isozymes, which is to be expected if each series is derived from a single gene product. Both results support the hypothesis that the primary products of the amylase loci undergo post-translational modifications. Salivary and pancreatic amylase appear to be immunologically identical.This investigation was supported in part by PHS Research Grant GM-19178.Supported by PHS Training Grant DE 119.Supported by PHS Training Grant GM 1056. |
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| Keywords: | amylase post-translational modification isozyme immunological purification |
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