Purification and Properties of Choriogonadotropin from Human Term Placenta
- 1 January 1977
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 358 (2) , 909-914
- https://doi.org/10.1515/bchm2.1977.358.2.909
Abstract
Affinity chromatography was applied successfully to the isolation of human choriogonadotropin from human term placenta. In a single step, a 57-fold purification was achieved. Evidence is presented which indicates that the product contains intact hormone as well as its free .alpha.-subunit. Preliminary data suggest that a variant form of .alpha.-subunit is also present which has serine at its N-terminal and contains relatively little arginine and proline compared to the authentic .alpha.-subunit.This publication has 4 references indexed in Scilit:
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- DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*Annals of the New York Academy of Sciences, 1964
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951