Comparison of LDH-B4 allozymes of macrourids (Teleostei: Gadiformes) by electrophoresis and peptide mapping

Raymond R. Wilson, University of South Florida St. Petersburg
Joseph F. Siebenaller, Louisiana State University
Bonnie J. Davis, Louisiana State University

Abstract

The heart-type lactate dehydrogenase (LDH-B4) homologs of two species of Nezumia and eight species of Coryphaenoides are isomobile on two commonly used electrophoretic buffer systems. To test the hypothesis that the homologs possess the same primary structures, the allozymes from N. bairdii and four species of Coryphaenoides were purified by affinity chromatography on an oxamate aminohexyl Sepharose column and digested with trypsin. The resulting peptide mixtures were then mapped using reversed-phase high-performance liquid chromatography. The peptide maps of the enzyme homologs indicate that the overall similarity of the homologs is high, but unique peptides in each species indicate that the allozymes are not identical in primary structure. © 1991.