DETERMINATION OF THE DISULFIDE ARRAY IN SAPECIN, AN ANTIBACTERIAL PEPTIDE OF SARCOPHAGA-PEREGRINA (FLESH FLY)

被引：43

作者：

KUZUHARA, T ^{[1
]}

NAKAJIMA, Y ^{[1
]}

MATSUYAMA, K ^{[1
]}

NATORI, S ^{[1
]}

机构：

[1] UNIV TOKYO,FAC PHARMACEUT SCI,BUNKYO KU,TOKYO 113,JAPAN

来源：

JOURNAL OF BIOCHEMISTRY | 1990年 / 107卷 / 04期

关键词：

D O I：

10.1093/oxfordjournals.jbchem.a123077

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Sapecin is a 40-residue peptide containing 6 half-cystine residues. The disulfide structure of sapecin was determined by sequencing cystine-containing peptides obtained by digesting sapecin with thermolysin. Results showed that sapecin has a vortical structure fixed by 3 disulfide bonds between cysteine residues 3 and 30, 16 and 36, and 20 and 38, respectively, and that these disulfide bonds are essential for its antibacterial activity. © 1990 COPYRIGHT, 1990 BY THE JOURNAL OF BIOCHEMISTRY.

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页码：514 / 518

页数：5

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