Characterization of gamma-crystallins from eye lenses of shark: closer structural similarity to mammalian than other piscine gamma-crystallins?
Lens crystallins were isolated and characterized from sharks of the cartilaginous fishes. Four crystallin fractions corresponding to alpha-, beta H-, beta L- and gamma-crystallins, similar to those of mammalian crystallins, were obtained. The native molecular masses and subunit structures of these purified fractions were analyzed by gel permeation chromatography, SDS gel electrophoresis and isoelectric focusing, revealing the typical subunit compositions with various extents of heterogeneity in each orthologous crystallin class. Amino acid and N-terminal sequence analyses corroborate the identification and classification of crystallin classes based on electrophoresis. Unexpectedly, it was found that the amino acid composition and N-terminal sequence of shark gamma-crystallin are more closely related to those of bovine than carp gamma-crystallin. This finding may have some bearing on the divergence and specification of gamma-crystallins between the phylogenetic lines of mammals and fishes.
Chiou
S H
SH
Institute of Biochemical Sciences, National Taiwan University, Taipei, Republic of China.
D000595:Amino Acid Sequence; D000818:Animals; D002347:Carps; D002417:Cattle; D003459:Crystallins / Q000235:genetics / Q000302:isolation & purification*; D007908:Lens, Crystalline / Q000378:metabolism*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D012754:Sharks / Q000378:metabolism*; D013045:Species Specificity
D003459:Crystallins