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dc.contributor.authorButnev, Viktor Y.en_US
dc.contributor.authorGotschall, R. Russellen_US
dc.contributor.authorBaker, Vanda L.en_US
dc.contributor.authorMoore, William T.en_US
dc.contributor.authorGout, Peter W.en_US
dc.contributor.authorBousfield, George R.en_US
dc.date.accessioned2012-01-24T17:48:31Z
dc.date.available2012-01-24T17:48:31Z
dc.date.issued1996-07en_US
dc.identifier8895086en_US
dc.identifierHD 29047en_US
dc.identifier8217321en_US
dc.identifier.citationJournal of protein chemistry. 1996 Jul; 15(5): 413-26.en_US
dc.identifier.issn0277-8033en_US
dc.identifier.urihttp://dx.doi.org/10.1007/BF01886848
dc.identifier.urihttp://hdl.handle.net/10057/4127
dc.descriptionClick on the DOI link below to access the article (may not be free).en_US
dc.description.abstractGlycosylated equine prolactin (G-ePRL) and nonglycosylated ePRL were purified to homogeneity from side fractions obtained during isolation of LH/FSH from horse pituitaries. Both PRL forms were isolated together in high yield by the isolation procedure used for glycosylated porcine PRL/(G-pPRL) and pPRL, involving acetone extraction/precipitation, NaCl and isoelectric precipitation, and gel filtration. Purification of G-ePRL required additional Con A chromatography. The N-terminal amino acid sequencing for 32 cycles of G-ePRL and ePRL resulted in sequences identical to the known primary structure of ePRL. Based on MALDI mass spectrometry analysis and SDS-PAGE mobilities, G-ePRL and ePRL had estimated molecular weights of 25,000 and 23,000 Da, respectively. G-ePRL displayed only 60% of the immunoreactivity of ePRL in homologous radioimmunoassay. Using the Nb2 lymphoma cell bioassay, ePRL was found to have about 1/30th the mitogenic activity of bovine PRL; G-ePRL was approximately 1/10th as active as ePRL. Glycosylation of G-ePRL at Asn31 was confirmed by isolation and sequence analysis of an enzymatically derived G-ePRL glycopeptide spanning residues 29-37. Monosaccharide compositions of intact G-ePRL and this glycopeptide were very similar (Man3, GlcNAc2, GalNAc1, Fuc0.6, Gal0.2, NeuAc0.15) and resembled that of G-pPRL. The glycopeptide contained one sulfate residue as determined by ion chromatography after acid hydrolysis, indicating the presence of a sulfated monosaccharide. Comparative carbohydrate analysis of G-ePRL and other G-PRL preparations suggests that the functionally significant Asn31 carbohydrate unit is a fucosylated complex mono- and /or biantennary oligosaccharide terminating with a sulfated GalNAc residue and two or three Man residues.en_US
dc.description.sponsorshipNICHD NIH HHSen_US
dc.language.isoengen_US
dc.publisherSpringer New Yorken_US
dc.publisherSpringer New Yorken_US
dc.relation.ispartofseriesJournal of protein chemistryen_US
dc.sourceNLMen_US
dc.subjectComparative Studyen_US
dc.subjectResearch Support, U.S. Gov't, P.H.S.en_US
dc.subject.meshAmino Acids/analysisen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCell Division/drug effectsen_US
dc.subject.meshChromatography, Gelen_US
dc.subject.meshElectrophoresis, Polyacrylamide Gelen_US
dc.subject.meshGlycosylationen_US
dc.subject.meshHorsesen_US
dc.subject.meshMolecular Weighten_US
dc.subject.meshMonosaccharides/chemistryen_US
dc.subject.meshPituitary Gland/chemistryen_US
dc.subject.meshProlactin/chemistryen_US
dc.subject.meshTumor Cells, Cultureden_US
dc.subject.meshProlactin/isolation & purificationen_US
dc.subject.meshProlactin/pharmacologyen_US
dc.titleGlycosylated equine prolactin and its carbohydrate moietyen_US
dc.typeArticleen_US
dc.description.versionpeer revieweden_US
dc.rights.holderCopyright © 1996, Springer Netherlandsen_US


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