title: Lamprey 48-kDa lens protein represents a novel class of crystallins.
abstract: SDS-PAGE revealed a major Mr 48 000 polypeptide of pI around 8 in the water-soluble fraction of lamprey lenses. It occurs as a monomeric protein, and its amino acid composition and tryptic peptides show no resemblances to alpha-, beta-, gamma- or delta-crystallin. Immunoblotting with antiserum against the 48-kDa protein revealed an immunologically related polypeptide of similar Mr in reptiles, several birds and a fish, but showed no cross-reactivity with any other water-soluble lens component. The 48-kDa protein is not detected in many birds and fishes, and in the investigated mammals and amphibians.
mesh_terms: D000596:Amino Acids / Q000302:isolation & purification; D000818:Animals; D005075:Biological Evolution; D055598:Chemical Phenomena; D002621:Chemistry; D002850:Chromatography, Gel; D003459:Crystallins / Q000145:classification / Q000302:isolation & purification*; D005399:Fishes / Q000378:metabolism*; D007798:Lampreys / Q000378:metabolism*; D007908:Lens, Crystalline / Q000378:metabolism*; D010446:Peptide Fragments / Q000302:isolation & purification; D012995:Solubility; D013045:Species Specificity
chemical_list: D000596:Amino Acids; D003459:Crystallins; D010446:Peptide Fragments