The carbohydrate moiety of immunoglobulins: biosynthesis and function

dc.contributor.advisorKimball, Aubrey P.
dc.contributor.committeeMemberBartel, Allen H.
dc.contributor.committeeMemberGray, Horace B., Jr.
dc.contributor.committeeMemberHuggins, Sara E.
dc.contributor.committeeMemberClark, Wallis Hensman, Jr.
dc.creatorCronenberger, Jo Helen
dc.date.accessioned2022-09-19T20:43:08Z
dc.date.available2022-09-19T20:43:08Z
dc.date.copyright1972
dc.date.issued1972
dc.description.abstractA model immunological system was established. It was found to contain a pool of K-chains to which glucose would be added as 89% sialic acid at the site of the plasma membrane. Several immunosuppressive reagents were used and their effect upon glucose incorporation into K-chains was determined. Methylthioinosine periodate oxidation product was found to suppress intracellular attachment of carbohydrate to L-chains, but it did not affect the plasma membrane or extracellular incorporation. Puromycin inhibited both protein synthesis and carbohydrate attachment. Arabinosylcytosine showed no effect on either protein or glucose incorporation. Plasma membranes were isolated and used as a sialyltransferase source to attach sialic acid to desialyzed K-chains. The role of the sialic acid and ß-galactosidase residues in IgG was not in antibody specificity or activity as detected by complement fixation and hemagglutination inhibition titers. In IgM, the carbohydrate moiety appears to play a role in conformation of the pentamer. More interestingly, the mannose and glucosamine residues of the Fc region function in noncovalent association of monomers into a pentameric molecule.
dc.description.departmentBiology and Biochemistry, Department of
dc.format.digitalOriginreformatted digital
dc.format.mimetypeapplication/pdf
dc.identifier.other17970559
dc.identifier.urihttps://hdl.handle.net/10657/11403
dc.language.isoen
dc.rightsThis item is protected by copyright but is made available here under a claim of fair use (17 U.S.C. Section 107) for non-profit research and educational purposes. Users of this work assume the responsibility for determining copyright status prior to reusing, publishing, or reproducing this item for purposes other than what is allowed by fair use or other copyright exemptions. Any reuse of this item in excess of fair use or other copyright exemptions requires express permission of the copyright holder.
dc.titleThe carbohydrate moiety of immunoglobulins: biosynthesis and function
dc.type.dcmiText
dc.type.genreThesis
dcterms.accessRightsThe full text of this item is not available at this time because it contains documents that are presumed to be under copyright and are accessible only to users who have an active CougarNet ID. This item will continue to be made available through interlibrary loan.
thesis.degree.collegeCollege of Arts and Sciences
thesis.degree.departmentBiochemical and Biophysical Sciences, Department of
thesis.degree.disciplineBiochemical and Biophysical Sciences
thesis.degree.grantorUniversity of Houston
thesis.degree.levelDoctoral
thesis.degree.nameDoctor of Philosophy

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