Amino acid sequence around the thiolester of α2‐macroglobulin from plasma of the crayfish, Pacifastacus leniusculus

FEBS Letters

Söderhäll, Kenneth¹  Sottrup-Jensen, Lars²  Hall, Martin¹ 

[1] Department of Physiological Botany, University of Uppsala, Sweden;Department of Molecular Biology, University of Aarhus, DK-8000 Aarhus C, Denmark

关键词: Macroglobulin;    α2;    Protease inhibitor;    Plasma protein;    (Crustacea);    α2M;    α2-macroglobulin;    DFP;    diisopropyl fluorophosphate;    DTE;    dithioerythreitol;    HPLC;    high-performance liquid chromatography;    PTH;    phenylthiohydantoin;    SDS-PAGE;    SDS-polyacrylamide gel electrophoresis;    TPCK;    N-tosyl-L-phenylalanine chloromethyl ketone;   

DOI  :  10.1016/0014-5793(89)81019-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

α₂-Macroglobulin (α₂M) was isolated from plasma of the freshwater crayfish, Pacifastacus leniusculus, using ultracentrifugation, ion-exchange chromatography and gel filtration techniques. The Pacifastacus α₂M molecule (Pα₂M) was radioactively labeled in the thiol ester structure with iodo [¹⁴C]acetic acid in the presence of methylamine. After reduction and carboxymethylation of the protein, it was digested with trypsin. A ¹⁴C-labeled tryptic peptide was sequenced and contained an amino acid sequence very similar to other known thiol ester sequences from human α₂M and related proteins. The N-terminal sequence of Pα₂M was related to that recently determined for lobster α₂M [(1987) J. Biol. Chem. 262, 14606–14611].

【 授权许可】

Unknown