Pyruvate kinases of salmon: Purification and comparison with the isozymes from birds and mammals

✍ Scribed by Guderley, Helga ;Cardenas, Janet M.

• Publisher: John Wiley and Sons
• Year: 1980
• Tongue: English
• Weight: 998 KB
• Volume: 211
• Category: Article
• ISSN: 0022-104X
• DOI: 10.1002/jez.1402110208

✦ Synopsis

Abstract

Pyruvate kinase occurs as two major forms in coho salmon; the type M isozyme occurs primarily in muscle and heart, but type K has a more generalized tissue distribution, in parallel with the type K isozyme in other vertebrate systems. In order to assess the evolutionary relationships among the fish, avian, and mammalian isozymes of pyruvate kinase, we have purified the two isozymes from fish, have examined some of their physical properties, and have studied their immunological relationships to theavian and mammalian isozymes. Salmon type K is at least partially inactivated by antibody to bovine type L pyruvate kinase as well as by antibodies produced against chicken, bovine, and salmon type M isozymes. Salmon type M pyruvate kinase, on the other hand, is not significantly cross‐reactive with the bovine type L isozyme, but is at least partially inactivated by antibodies produced against bovine or chicken type M isozymes. Mammalian type L pyruvate kinase is immunologically distinct from either mammalian type K or type M, but salmon type K has some structural features in common with all three mammalian isozymes. Thus, salmon fish type K pyruvate kinase could be similar to a primordial form that was antecedent to the three major differentiated isozymes of higher vertebrates.