AMINO-ACID-SEQUENCE AND DISULFIDE BRIDGES OF AN ANTIFUNGAL PROTEIN ISOLATED FROM ASPERGILLUS-GIGANTEUS

被引：63

作者：

NAKAYA, K

OMATA, K

OKAHASHI, I

NAKAMURA, Y

KOLKENBROCK, H

ULBRICH, N

机构：

[1] FREE UNIV BERLIN,INST BIOCHEM,OSTPREUSSENDAMM 111,W-1000 BERLIN 45,GERMANY

[2] SHOWA UNIV,SCH PHARMACEUT SCI,BIOL CHEM LAB,TOKYO 142,JAPAN

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1990年 / 193卷 / 01期

关键词：

D O I：

10.1111/j.1432-1033.1990.tb19300.x

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：

A very basic secreted protein whch displays antifungal activity was isolated from the medium of the mold Aspergillus giganteus. The protein consists of 51 amino acid residues whose sequence was determined as Ala ‐Thr‐Tyr‐Asn‐Gly‐Lys‐Cys‐Tyr‐Lys‐Lys‐Asp‐Asn‐Ile‐Cys‐Lys‐Tyr‐Lys‐Ala‐Gln‐Ser‐Gly‐Lys‐Thr‐Ala‐Ile‐Cys‐Lys‐Cys‐Tyr‐Val‐Lys‐Lys‐Cys‐Pro‐Arg‐Asp‐Gly‐Ala‐Lys‐Cys‐Glu‐Phe‐Asp‐Ser‐Tyr‐Lys‐Gly‐Lys‐Cys‐Tyr‐Cys. Disulfide bonds were formed between Cys7–Cys33, Cys14–Cys40, Cys26–Cys28 and Cys49–Cys51. These results suggest that the antifungal protein forms a loop structure and is similar to phospholipase A2. Copyright © 1990, Wiley Blackwell. All rights reserved

引用

页码：31 / 38

页数：8