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

Autor: Karn, R. C., Rosenblum, Barnett B., Ward, Jewell C., Merritt, A. Donald, Shulkin, Jeff D.
Zdroj: Biochemical Genetics; December 1974, Vol. 12 Issue: 6 p485-499, 15p
Abstrakt: 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.
Databáze: Supplemental Index