The amino-terminal sequences of four major carp gamma-crystallin polypeptides and their homology with frog and calf gamma-crystallins.
Four major gamma-crystallin subfractions have been isolated from the carp (Cyprinus carpio) and their N-terminal sequences determined by Edman protein sequencing. Extensive homologies indicative of close relatedness in their primary structure were found in these four gamma-crystallin polypeptides. Comparison of the carp N-terminal sequences with those of mammalian and amphibian gamma-crystallins also showed a high degree of homology present in their N-terminal segments despite the dissimilarity of amino acid compositions of fish gamma-crystallins to those of higher classes of vertebrates. The distinct yet closely-related partial sequences of carp gamma-crystallins could account for the profound microheterogeneity detected in the characterization of carp crystallins, suggesting the presence of a multigene family for gamma-crystallin in the lowest class of vertebrates, i.e. the fish.
D000595:Amino Acid Sequence; D000818:Animals; D002347:Carps / Q000235:genetics*; D003459:Crystallins / Q000235:genetics* / Q000302:isolation & purification; D003530:Cyprinidae / Q000235:genetics*; D011898:Ranidae / Q000235:genetics; D051381:Rats; D012689:Sequence Homology, Nucleic Acid; D013045:Species Specificity
D003459:Crystallins