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 Biochemjournal_title
Journal of biochemistryauthors
Kimura H,Murata H,Uematsu Hdoi
10.1093/oxfordjournals.jbchem.a132985subject
Has Abstractpub_date
1980-08-01 00:00:00pages
395-401issue
2eissn
0021-924Xissn
1756-2651journal_volume
88pub_type
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更新日期:1980-11-01 00:00:00
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journal_title:Journal of biochemistry
pub_type: 杂志文章
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journal_title:Journal of biochemistry
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doi:
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