Immunological relationships and post-translational modifications of human salivary amylase (Amy1) and pancreatic amylase (Amy2) isozymes

✍ Scribed by R. C. Karn; Barnett B. Rosenblum; Jewell C. Ward; A. Donald Merritt; Jeff D. Shulkin

• Publisher: Springer
• Year: 1974
• Tongue: English
• Weight: 868 KB
• Volume: 12
• Category: Article
• ISSN: 0006-2928
• DOI: 10.1007/bf00486066

✦ Synopsis

Electrophoretic phenotypes of human salivary amylase (Amy j) and pancreatic amylase (Amyz) consist of complex isozyme patterns which may result from posttranslational 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 Amy 2 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.