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Immunological relationships and post-translational modifications of human salivary amylase (Amy1) and pancreatic amylase (Amy2) isozymes
Authors:R C Karn  Barnett B Rosenblum  Jewell C Ward  A Donald Merritt  Jeff D Shulkin
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
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.
Keywords:amylase  post-translational modification  isozyme  immunological  purification
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