Lamprey 48‐kDa lens protein represents a novel class of crystallins

FEBS Letters

de Jong, Wilfried W.¹  Stapel, Steven O.¹ 

[1] Laboratorium voor Biochemie, Universiteit van Nijmegen, Geert Grooteplein Noord 21, 6525 EZ Nijmegen, The Netherlands

关键词: Crystallin;    Lens protein;    Lamprey;    Protein evolution;    Immunoblotting;   

DOI  :  10.1016/0014-5793(83)80777-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown