On the phosphorylation of low molecular mass HMG (high mobility group) proteins in Ehrlich ascites cells

This paper shows that the low molecular mass HMG proteins 14 and 17 do not seem to be phosphorylated in Ehrlich ascites cells whereas two other small HMG proteins designated HMG I and Y are. Amino acid analysis and peptide mapping of all four proteins demonstrated that HMG I and Y were not phosphory...

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Veröffentlicht in:	FEBS letters 1985-01, Vol.180 (2), p.275-279
Hauptverfasser:	Lund, T., Holtlund, J., Laland, S.G.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acids - analysis Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Carcinoma, Ehrlich Tumor - metabolism Cell Line Ehrlich ascites tumor cells Electrophoresis, Polyacrylamide Gel Endopeptidases - metabolism Fundamental and applied biological sciences. Psychology high mobility group proteins High Mobility Group Proteins - metabolism HMG protein Holoproteins Mice Nuclear proteins peptide mapping Phosphorylation Proliferating cell Proteins Serine Endopeptidases
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Zusammenfassung:	This paper shows that the low molecular mass HMG proteins 14 and 17 do not seem to be phosphorylated in Ehrlich ascites cells whereas two other small HMG proteins designated HMG I and Y are. Amino acid analysis and peptide mapping of all four proteins demonstrated that HMG I and Y were not phosphorylated modifications of HMG 14 or 17.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/0014-5793(85)81085-1