Literature DB >> 3964268

Labile oligomeric structure of human placental 15-hydroxyprostaglandin dehydrogenase.

T Tanaka, T Kotani, S Ohtaki, K Nagai, K Tsuruta, N Mori.   

Abstract

NAD-dependent 15-hydroxyprostaglandin dehydrogenase has been isolated from human term placenta. About 9,000-fold enrichment was achieved with a yield of 7.6%. Electrophoretic analyses suggested that glycerol stabilized an active structure of the enzyme, and sodium dodecyl sulfate might dissociate it. The instability of the enzyme activity may relate to its labile oligomeric structure which is easily dissociated into subunits.

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Year:  1986        PMID: 3964268     DOI: 10.1016/0006-291x(86)91035-1

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  1 in total

1.  Monoclonal antibodies that inhibit the enzyme activity of NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase.

Authors:  C L Tai; O T Mak; T Arai; H H Tai
Journal:  Biochem J       Date:  1990-04-01       Impact factor: 3.857

  1 in total

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