Publication Date

1987

Document Type

Dissertation/Thesis

First Advisor

Conway, Thomas P.

Degree Name

M.S. (Master of Science)

Department

Department of Biological Sciences

LCSH

Blood proteins||Glycoproteins||Monoclonal antibodies

Abstract

Heme and metals are bound to specific serum proteins for transport in the serum. Histidine-Rich Glycoprotein (HRG), MW 94,000, does not have a well-defined physiological role, although it is thought to function in divalent metal transport and fibrin clotting. Hemopexin (Hx), MW 60,000, binds heme released from hemoglobin and transports it to the liver, where the heme-hemopexin complex is bound to specific receptors on the hepatocyte membrane. Cleavage of Hx with plasmin produces two peptides. Domain I, MW 35,000, binds heme, whereas domain II, MW 25,000, does not. In order to further study the function of HRG and Hx, two monoclonal antibodies were produced to rabbit HRG, and eight monoclonal antibodies were produced to rabbit Hx. Competitive binding assays with anti-Hx monoclonals indicate that four bound antigenic determinants on Hx and domain I, one bound an antigenic determinant on Hx and domain II, and two bound antigenic determinants on Hx only.

Comments

Bibliography: pages [64]-69.

Extent

69 pages

Language

eng

Publisher

Northern Illinois University

Rights Statement

In Copyright

Rights Statement 2

NIU theses are protected by copyright. They may be viewed from Huskie Commons for any purpose, but reproduction or distribution in any format is prohibited without the written permission of the authors.

Media Type

Text

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