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PMID: 667064 Published · ppublish English Journal Article

Studies on the degradation of high mobility group non-histone chromosomal proteins.

Biochimica et biophysica acta ·Vol. 519 ·No. 1 ·1978-06-22 ·Pages 233-42

Goodwin GH, Walker JM, Johns EW

Abstract

During the isolation of high mobility group non-histone proteins from calf thymus chromatin by methods described previously (e.g. Goodwin, G.H., Nicolas, R.H. and Johns, E.W. (1975) Biochim. Biophys, Acta. 405, 280--291) protein degradation occurs resulting in a number of proteins appearing in the chromatin extracts which are not present in high mobility group protein preparations in which proteolysis has been completely inhibited. These extra proteins, formerly numbered high mobility group proteins 3, 5, 6 and 8, are thus probably degradation products of other nuclear proteins, produced during the isolation procedure. From the amino acid analyses, tryptic peptides and N-terminal sequences, it is concluded that high mobility group protein 3 is probably a degradation product of high mobility group protein 1. The amino acid analysis of high mobility group protein 8 is very similar to that of the N-terminal half of histone H1 suggesting that high mobility group protein 8 is a degradation product of this histone.

MeSH Terms
Amino Acids/analysis Animals Cattle Chromatin/analysis Chromosomal Proteins, Non-Histone/analysis,isolation & purification,metabolism Histones/metabolism Hydrolysis Isoelectric Point Molecular Weight Peptide Fragments/analysis Thymus Gland
Chemicals
Amino Acids Chromatin Chromosomal Proteins, Non-Histone Histones Peptide Fragments
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Goodwin G H
Walker J M
Johns E W
Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
1978-06-22
Pages
233-42
Language
English
Region
Netherlands
NLM ID
0217513
Subset
IM
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