Purification and characterization of ubiquitin from mammalian testis

Ubiquitin was extracted from testis of 4 mammals and purified to homogeneity by gel filtration chromatography. Amino acid compositions and NH 2-terminal sequences were found to be identical in the 4 species and with calf thymus ubiquitin. Ubiquitin conformation was shown to be very sensitive to oxid...

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Veröffentlicht in:	FEBS letters 1984-04, Vol.169 (2), p.199-204
Hauptverfasser:	Loir, M., Caraty, A., Lanneau, M., Menezo, Y., Muh, J.P., Sautiere, P.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino acid analysis Amino Acid Sequence Amino Acids - analysis Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Chromatography, Gel Chromosomal Proteins, Non-Histone - isolation & purification Fundamental and applied biological sciences. Psychology Gel filtration chromatography Holoproteins Male Mammalia Mammalian testis Mammals Nuclear proteins Nucleoproteins - isolation & purification Oxidation-Reduction Protein Conformation Proteins Radioimmunoassay testes Testis - analysis ubiguitin Ubiquitin Ubiquitins
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Beschreibung
Zusammenfassung:	Ubiquitin was extracted from testis of 4 mammals and purified to homogeneity by gel filtration chromatography. Amino acid compositions and NH 2-terminal sequences were found to be identical in the 4 species and with calf thymus ubiquitin. Ubiquitin conformation was shown to be very sensitive to oxidation. Improved methods for radioimmunoassay of ubiquitin in tissue extracts are also discussed.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/0014-5793(84)80318-X