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Medientyp:
E-Artikel
Titel:
Human Luteinizing Hormone : Isolation and Characterization of the Native Hormone and Its α and β Subunits
:
Isolation and Characterization of the Native Hormone and Its α and β Subunits
Beteiligte:
CLOSSET, Jean;
VANDALEM, Jean‐Louis;
HENNEN, Georges;
LEQUIN, Rudy M.
Erschienen:
Wiley, 1975
Erschienen in:
European Journal of Biochemistry, 57 (1975) 2, Seite 325-333
Beschreibung:
A new procedure is described for the isolation of the α and β chains of the hormone. In this method, the native hormone is incubated in acidic urea and the chains are then separated by ion‐exchange chromatography.The amino‐terminal residue of the α subunit is valine. The carboxy‐terminal end of the α subunit is of variable length. No amino‐terminal residue was detected for the β chain; glycine was found at its carboxy‐terminal end by the selective titration method.The amino acid and carbohydrate compositions of the hormone and both subunits are presented. The β chain contains sialic acid and is devoid of galactosamine in contrast to the β subunits of other species.Contamination of our human lutenizing hormone preparation by other pituitary glycoprotein hormones such as thyroid‐stimulating hormone and follicle‐stimulating hormone amounted to 0.5 and 0.25 percent by weight respectively.Cross‐contamination of the initial α and β subunit preparations was measured by specific radioimmunoassays and amounted to 4.1 and 2 percent by weight respectively.Further extensive purification of these subunit preparations was then performed by means of affinity chromatography using immunosorbants.The final preparations exhibited a residual cross‐contamination amounting to 0.2 and 0.02 percent by weight for the α and β subunits respectively.