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Lamprey 48‐kDa lens protein represents a novel class of crystallins
Author(s) -
Stapel Steven O.,
de Jong Wilfried W.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80777-7
Subject(s) - crystallin , lamprey , lens (geology) , antiserum , biology , biochemistry , molecular mass , monomer , chemistry , antibody , enzyme , genetics , fishery , paleontology , organic chemistry , polymer
SDS—PAGE revealed a major M r 48000 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 α‐, β‐, γ‐ or δ‐crystallin. Immunoblotting with antiserum against the 48‐kDa protein revealed an immunologically related polypeptide of similar M r 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.