tau-Crystallin from the turtle lens: purification and partial characterization.
A lens protein with a molecular mass near 46 000 daltons has been purified from the turtle lens. It is a monomeric protein which differs from other lens crystallins in its antigenicity, near-UV circular dichroism spectrum and amino acid composition. Like delta-crystallin, it has appreciable secondary structure (52% alpha-helix). This lens protein has been named tau-crystallin. tau-Crystallin cross-reacts with the novel 48 000 dalton protein identified recently in lenses of the sea lamprey. Although distinct, the possibility that tau-crystallin shares an ancestral relationship with delta-crystallin is discussed.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002942:Circular Dichroism; D003459:Crystallins / Q000302:isolation & purification*; D007908:Lens, Crystalline / Q000032:analysis*; D008970:Molecular Weight; D011487:Protein Conformation; D014426:Turtles / Q000378:metabolism*
D000596:Amino Acids; D003459:Crystallins