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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Institution: | (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 Amy
1 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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