Disulfide bonds of purothionine, a lethal toxin for yeasts.

Abstract:

:Purothionin isolated from commercial wheat flour contained several components and two of them (A-I and A-II) were isolated in pure form by CM-52 column chromatography. Each component contained 45 amino acid residues with a 4 disulfide bonds. Purothionin A-II was digested with trypsin and thermolysin to isolate cystine peptides. These were separated and purified by chromatography on an SP-Sephadex column, and paper electrophoresis and chromatography. A peptide containing a -Cys-Cys- sequence was hydrolyzed with 10 N sulfuric acid. Amino acid compositions and partial sequence studies of the cystine peptides and their performic acid-oxidized peptides revealed the positions of all 4 disulfide bonds in purothionin A-II. They were formed between residues 3 and 39, 4 and 31, 12 and 29, and 16 and 25. The results of a partial study of purothionin A-I are also presented.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Hase T,Matsubara H,Yoshizumi H

doi

10.1093/oxfordjournals.jbchem.a132079

subject

Has Abstract

pub_date

1978-06-01 00:00:00

pages

1671-8

issue

6

eissn

0021-924X

issn

1756-2651

journal_volume

83

pub_type

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