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dc.contributor.authorButnev, Vladimir Y.en_US
dc.contributor.authorSingh, Vinoden_US
dc.contributor.authorNguyen, Van T.en_US
dc.contributor.authorBousfield, George R.en_US
dc.identifierAG15428/ DK52383en_US
dc.identifier.citationThe Journal of endocrinology. 2002 Mar; 172(3): 545-55.en_US
dc.descriptionClick on the DOI link below to access the article (may not be free).en_US
dc.description.abstractHybrid hormone preparations were prepared by combining intact and Asn(56)-deglycosylated (N(56)dg) equine (e) LH or FSH alpha subunit preparations with truncated, des(121-149)eLH beta (eLH beta t), immunopurified, intact eLH beta or equine chorionic gonadotropin beta (eCG beta) preparations, and eFSH beta. The LH receptor-binding potencies of N(56)dg-eLH alpha:eLH beta t and N(56)dg-eFSH alpha:eLH beta t hybrids were equivalent to that of eLH; however, both N(56)dg-alpha preparations were only 3-4% as active as eLH in the rat testis Leydig cell bioassay. In the granulosa cell FSH bioassay, eLH alpha:eLH beta t stimulated progesterone synthesis and induced aromatase activity, while N(56)dg-eLH alpha:eLH beta t was completely inactive at doses up to 5 microg. N(56)dg-eLH alpha:eLH beta t inhibited progesterone production and aromatase induction elicited by 0.3 ng eFSH or 2 ng human (h) FSH. The inhibitory activities of N(56)dg-eLH alpha:eLH beta and N(56)dg-eCG alpha:eLH beta t were only 10% that of N(56)dg-eLH alpha:eLH beta t. N(56)dg-eLH alpha:eCG beta did not inhibit progesterone synthesis stimulated by eFSH at all and appeared to further stimulate aromatase induction at the highest dose tested. Preincubation of N(56)dg-eLH alpha:eLH beta and N(56)dg-eLH alpha:eLH beta t for 72 h at 37 C resulted in no loss of FSH receptor-binding activity. Preincubation resulted in 50% loss of receptor-binding activity by the eFSH preparation due to subunit dissociation, while 88% of N(56)dg-eLH alpha:eFSH beta activity was lost following 72 h, 37 C preincubation. While alpha Asn(56) oligosaccharide had no effect on eLH beta hybrid stability, it did contribute to the stability of the eFSH heterodimer.en_US
dc.description.sponsorshipNIA NIH HHS/ NIDDK NIH HHSen_US
dc.publisherBioScientifica Ltd.en_US
dc.relation.ispartofseriesThe Journal of endocrinologyen_US
dc.subjectResearch Support, U.S. Gov't, Non-P.H.S.en_US
dc.subjectResearch Support, U.S. Gov't, P.H.S.en_US
dc.subject.meshDose-Response Relationship, Drugen_US
dc.subject.meshFollicle Stimulating Hormone/antagonists & inhibitorsen_US
dc.subject.meshGlycoprotein Hormones, alpha Subunit/metabolismen_US
dc.subject.meshGranulosa Cells/drug effectsen_US
dc.subject.meshLuteinizing Hormone/chemistryen_US
dc.subject.meshRadioligand Assay/methodsen_US
dc.subject.meshRecombinant Proteins/metabolismen_US
dc.subject.meshGlycoprotein Hormones, alpha Subunit/metabolismen_US
dc.subject.meshGranulosa Cells/metabolismen_US
dc.subject.meshLuteinizing Hormone/metabolism*en_US
dc.titleTruncated equine LH beta and asparagine(56)-deglycosylated equine LH alpha combine to produce a potent FSH antagonisten_US
dc.description.versionpeer revieweden_US
dc.rights.holderCopyright @ 2002 Society for Endocrinologyen_US

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