Reconstitution of horse heart cytochrome c: reformation of the peptide bond linking residues 65 and 66.

Details

Serval ID
serval:BIB_85F8933BBDCF
Type
Article: article from journal or magazin.
Collection
Publications
Title
Reconstitution of horse heart cytochrome c: reformation of the peptide bond linking residues 65 and 66.
Journal
Biochemical and Biophysical Research Communications
Author(s)
Corradin G., Harbury H.A.
ISSN
0006-291X (Print)
ISSN-L
0006-291X
Publication state
Published
Issued date
1974
Volume
61
Number
4
Pages
1400-1406
Language
english
Abstract
Horse heart cytochrome c can be treated with cyanogen bromide under conditions resulting in division of the molecule into a heme peptide of 65 residues and a peptide of 39 residues, corresponding to segments 1-65 and 66-104 of the parent protein, respectively. Upon mixture of the two peptides in aqueous solution, a complex can be formed that is slowly converted to a product with properties nearly indistinguishable from those of the initial heme protein. Evidence is presented that in this slow phase of the reaction the fragments are rejoined into a continuous chain through restoration of the peptide bond linking residues 65 and 66.
Keywords
Amino Acid Sequence, Animals, Chromatography, Gel, Cyanogen Bromide, Cytochrome c Group/metabolism, Heme/analysis, Horses, Myocardium/enzymology, Peptide Fragments, Protein Binding
Pubmed
Web of science
Create date
24/01/2008 15:55
Last modification date
20/08/2019 15:45
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