Please use this identifier to cite or link to this item: https://hdl.handle.net/20.500.12202/2694
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dc.contributor.authorKREAM, RICHARD M.
dc.date.accessioned2018-07-12T18:08:46Z
dc.date.available2018-07-12T18:08:46Z
dc.date.issued1981
dc.identifier.citationSource: Dissertation Abstracts International, Volume: 41-12, Section: B, page: 4502.
dc.identifier.urihttps://ezproxy.yu.edu/login?url=http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&res_dat=xri:pqm&rft_dat=xri:pqdiss:8111882
dc.identifier.urihttps://hdl.handle.net/20.500.12202/2694
dc.description.abstractA radioiodinated form of the highly potent enkephalin analog FK 33-824 has been characterized with respect to its binding properties in vitro. ('125)I-FK 33-824 is distinctive among the short opioid peptides in three ways. First, ('125)I-FK 33-824 binds stereospecifically to rat brain homogena.
dc.publisherProQuest Dissertations & Theses
dc.subjectBiochemistry.
dc.titleBIOCHEMICAL STUDIES OF THE MAMMALIAN AND INVERTEBRATE OPIATE RECEPTOR
dc.typeDissertation
Appears in Collections:Albert Einstein College of Medicine: Doctoral Dissertations

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