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PMID: 206657 Published · ppublish English Comparative Study Journal Article

Controlled proteolytic digestion of the M-protein of Sendai virus: the isolation of a fragment of 30000 molecular weight.

The Journal of general virology ·Vol. 39 ·No. 2 ·1978-05-00 ·Pages 311-9

Hewitt JA, Allen G

Abstract

Proteolytic digestion of the M-protein of Sendai virus produces a product with a mol. wt. approximately 5000 less than that of the intact protein. In the case of digestion with chymotrypsin this cleavage is quite specific and the cleaved protein can be isolated. The smaller fragment appears to be physically removed from the larger (30000 mol. wt.) fragment, rather than remaining in non-covalent association with it. The cleavage is likely to be near the N-terminus of the protein. At the present time there is no indication of the biological function of this fragment.

MeSH Terms
Amino Acids/analysis Chymotrypsin/metabolism Molecular Weight Parainfluenza Virus 1, Human/analysis,metabolism Trypsin/metabolism Viral Proteins/analysis,isolation & purification,metabolism
Chemicals
Amino Acids Viral Proteins Chymotrypsin Trypsin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Hewitt J A
Allen G
Article Info
Journal
The Journal of general virology
Abbr.
J Gen Virol
ISSN
0022-1317
Published
1978-05-00
Pages
311-9
Language
English
Region
England
NLM ID
0077340
Subset
IM
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