Amino acid sequence of a 32‐residue region around the thiol ester site in duck ovostatin

FEBS Letters

Nagase, Hideaki²  Brew, Keith¹ 

[1] Department of Biochemistry, University of Miami School of Medicine, Miami, FL 33101, USA;Department of Biochemistry, University of Kansas Medical Center, Kansas City, KS 66103, USA

关键词: Ovostatin;    α2-Macroglobulin;    Thiol ester;    Amino acid sequence;   

DOI  :  10.1016/0014-5793(87)80196-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

To obtain the amino acid sequence at the thiol ester site in duck ovostatin for comparisons with other proteins, the native ovostatin was labeled with ¹⁴CH₃NH₂ at the reactive thiol ester site. The modified protein was reduced, carboxymethylated, and digested with trypsin. ¹⁴C-labeled peptides isolated by gel filtration with Sephadex G-50, ion-exchange chromatography on DEAE-cellulose and HPLC were subjected to automated sequence analysis, and the stretch of 32 amino acid residues containing the ¹⁴CH₃NH₂-binding site were determined. A comparison of this sequence with the corresponding sequences in α₂-macroglobulin, and complement components C3 and C4 revealed 72, 31 and 34% homology, respectively. The results indicate that ovostatin is a close relative to plasma α-macroglobulins and may share a common ancestor with C3 and C4.

【 授权许可】

Unknown