Sequence analysis of peptide fragments from the intrinsic membrane protein of calf lens fibers MP26 and its natural maturation product MP22

FEBS Letters

Ngoc, Lien Do¹  Hoebeke, Johan²  Paroutaud, Pierre²  Dunia, Irene¹  Benedetti, E.Lucio¹ 

[1] Laboratory of Electron Microscopy, University of Paris VII, 2, Place Jussieu, F75251-Paris Cédex 05, France;Molecular Immunology, Institut Jacques Monod, CNRS, University of Paris VII,2, Place Jussieu, F75251-Paris Cédex 05, France

关键词: Intrinsic lens fiber membrane protein;    Bovine lens;    Amino acid sequence;    MP26;    intrinsic membrane protein of calf lens fibers;    MP22;    maturation product of MP26;    MP22T;    trypsin fragment of MP26;    MP22V8;    protease V8 fragment of MP26;    C15K;    CNBr fragment of MP26;    C11K;    CNBr fragment of MP22;    PAGE;    polyacrylamide gel electrophoresis;    TPCK;    1-1-tosylamide-2-phenylethyl chloromethyl ketone;   

DOI  :  10.1016/0014-5793(85)81116-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Calf lens fiber plasma membranes, containing only the intrinsic membrane protein MP26 and its maturation product MP22 were treated with proteolytic enzymes such as trypsin, protease V8 from S. aureus or with chemical agents as CNBr in formic acid. The cleavage products, purified by electrophoresis, were analysed for their amino acid composition and N-terminal sequences. Proteolysis gave rise to peptides which were mainly shortened at the C-terminal end of the molecules. While the V8 protease produced a fragment with a similar N-terminal sequence as the maturation product MP22, trypsin yielded another cleavage product. Chemical hydrolysis yielded large fragments (11–15 kDa) with hydrophobic N-terminal sequences. Our results suggest that MP26 is characterised by an N-terminal signal sequence and possesses other hydrophobic domains which could function as untranslocated insertion sequences.

【 授权许可】

Unknown