Chemical modification or excision of neurophysin arginine-8 is associated with loss of peptide-binding ability

The role of neurophysin arginines in the binding of peptides to the principal hormone-binding site was evaluated by modification of neurophysin with cyclohexanedione and by limited proteolysis with trypsin. Binding affinities were reduced to values less than 3% of normal when both Arg-8 and Arg-20 w...

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Published inBiochemical and biophysical research communications Vol. 106; no. 1; pp. 194 - 201
Main Authors Breslow, Esther, Pagnozzi, Martin, Rochester Tiao-te Co
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 14.05.1982
Subjects
Amino Acids - analysis
Animals
Arginine
Cattle
chemical modification
Cyclohexanones
neurophysin
Neurophysins
peptides
Protein Binding
Trypsin
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Summary:The role of neurophysin arginines in the binding of peptides to the principal hormone-binding site was evaluated by modification of neurophysin with cyclohexanedione and by limited proteolysis with trypsin. Binding affinities were reduced to values less than 3% of normal when both Arg-8 and Arg-20 were chemically modified or when residues 1–8 were excised by trypsin. Because residues 1–6 are non-essential to binding and residue 7 is not conserved in evolution, the results are interpreted in terms of a functional role for Arg-8.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(82)92077-0