Studies on the degradation of high mobility group non-histone chromosomal proteins.
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.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D002843:Chromatin / Q000032:analysis*; D002868:Chromosomal Proteins, Non-Histone / Q000032:analysis* / Q000302:isolation & purification / Q000378:metabolism; D006657:Histones / Q000378:metabolism; D006868:Hydrolysis; D007526:Isoelectric Point; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D013950:Thymus Gland
D000596:Amino Acids; D002843:Chromatin; D002868:Chromosomal Proteins, Non-Histone; D006657:Histones; D010446:Peptide Fragments