Increase in the susceptibility of hemoglobin to trypsin on treatment with glutathione or cysteine.

Abstract:

:1. Native human hemoglobin A was digested with proteases after treatment with reduced or oxidized glutathione, cysteine, or cystine. 2. The treatment of hemoglobin with a 40-fold molar excess of reduced glutathione or cysteine at 37 degrees C for 4 enhanced its susceptibility to trypsin 4 or 6 times, respectively. However, oxidized glutathione and cystine had little or no effect on its susceptibility to the protease. 3. The enhanced susceptibility was not due to conformational change in hemoglobin, such as dissociation to dimers or monomers, or to unfolding of alpha-helical structure, but was due to dissociation of heme from the globin moiety, judging from measurements of the absorption spectrum and circular dichroism spectrum, and gel-filtration analysis.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Kimura H,Murata H,Uematsu H

doi

10.1093/oxfordjournals.jbchem.a132985

subject

Has Abstract

pub_date

1980-08-01 00:00:00

pages

395-401

issue

2

eissn

0021-924X

issn

1756-2651

journal_volume

88

pub_type

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