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Updated: Aug 11, 2026

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography
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Published on: March 10, 2010

[Isolation of "pregnancy-zone" proteins using immuno absorbents and study of possible enzyme activities]

W Straube, R Hofmann, B Klausch

    Zentralblatt Fur Gynakologie
    |January 1, 1975
    PubMed

    The purification of the pregnancy zone protein by means of immunoadsorbents is described. The pregnancy zone protein antibody was isolated from an absorbed rabbit antiserum and coupled with CNBr-activated sepharose. The pregnancy zone protein was isolated from pregnancy serum by the specific antibody cross-linked with sepharose. Contaminating serum proteins were eliminated by "inverse" immunoadsorption using antibodies against these proteins coupled with sepharose. An immunoelectrophoretically pure pregnancy zone protein was obtained. By means of a combination of immunoprecipitation and enzyme reaction in agar gel could be excluded that the pregnancy zone protein possesses activities of the following 11 enzymes: ceruloplasmin, leucine amino peptidase, alkaline phosphatase, carboxylic esterase, lactate dehydrogenase, malate dehydrogenase, glycerophosphate dehydrogenase, glucose-6-phosphat-dehydrogenase, cholinesterase, acetyl cholinesterase and oxytocinase.

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