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dc.contributor.advisorJackson, Richard L.
dc.contributor.authorFletcher, Geralyn M.
dc.date.accessioned2011-07-27T18:21:25Z
dc.date.available2011-07-27T18:21:25Z
dc.date.issued1984
dc.identifier.urihttp://hdl.handle.net/10920/22950
dc.descriptionv, 40 p.en_US
dc.description.abstractLipoprotein lipase (LpL) is the enzyme responsible for the hydrolysis of the triglycerides of chylomicrons and very-low- density lipoproteins (VLDL). Heparin has been shown to release LpL from its normal site on the lumenal capillary endothelium, facilitating its hydrolytic activity. Heparin has also been found to affect LpL-catalyzed triglyceride hydrolysis in vitro; it is believed that it exerts this effect by binding to the LpL. In this study crude heparin from, porcine intestinal mucosa was fractionated according to its affinity for bovine milk LpL and that fraction which bound most tightly, designated "HRH" (highly reactive heparin), was isolated and partially characterized. It was found to precipitate low-density lipoprotein (LDL) as effectively as heparin isolated solely for this ability. LpL incubated with HRH retained up to 31.3% more of its catalytic activity in p-nitrophenyl butyrate hydrolysis than LpL incubated alone. Heparin with little affinity (URH, or unreactive heparin) for LpL had much less of an effect on Lpl activity. It was found that radioactively labelling HRH with 125 I left it unable to bind LpL in affinity chromatography and in a ligand-blotting assay. It is suggested that there exists a small fraction of crude heparin which is capable of interacting with lipoprotein lipase; further characterization of this fraction may prove useful in studies of lipoprotein metabolism.en_US
dc.format.mimetypeapplication/pdf
dc.language.isoen_USen_US
dc.publisherKalamazoo Collegeen_US
dc.relation.ispartofKalamazoo College Biology Senior Individualized Projects Collection
dc.relation.ispartofseriesSenior Individualized Projects. Biology;
dc.rightsU.S. copyright laws protect this material. Commercial use or distribution of this material is not permitted without prior written permission of the copyright holder.
dc.titleIsolation and Partial Characterization of a Heparin Fraction Specific for Binding of Bovine Milk Lipoprotein Lipaseen_US
dc.typeThesisen_US
KCollege.Access.ContactIf you are not a current Kalamazoo College student, faculty, or staff member, email dspace@kzoo.edu to request access to this thesis.


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  • Biology Senior Individualized Projects [1520]
    This collection includes Senior Individualized Projects (SIP's) completed in the Biology Department. Abstracts are generally available to the public, but PDF files are available only to current Kalamazoo College students, faculty, and staff.

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