Date of Award

Spring 1980

Document Type

Thesis

Degree Name

Master of Science (MS)

Department

Chemistry & Biochemistry

Program/Concentration

Chemistry

Committee Director

Roy L. Williams

Committee Member

David Brase

Committee Member

Thomas O. Stiz

Committee Member

Billy T. Upchurch

Call Number for Print

Special Collections LD4331.C45H35

Abstract

Cerebroside sulfate (CS) has recently been shown to bind opiate drugs in a pharmacologically relevent manner and therefore satisfy the structural requirements of an opiate receptor. Seminolipid (SGG), a novel sulfated galactosyl. glycerolipid that has been isolated from the testes of a variety of mammals, may be viewed as a structural analog of CS. In view of this structural similarity, it is reasonable to presume that SGG may also bind opiate drugs. The isolation of SGG from boar testes was accomplished using silica gel dry column chromotography with a chloroform: methanol water solvent system. The structure and purity of the isolated SGG were proven by infra-red and thin layer chromotography, respectively. Two methods were used to evaluate the opiate binding potential of SGG compared to that of CS: first, a modified sulfatide analysis using azure-A dye (the Kean test), and second, 3H-opiate binding studies on the brains and testes of rats and mice, and boar testes. Both of these in vitro methods of opiate binding evaluation failed to reveal opiate binding comparable to CS that could be attributed to SGG contained in the testes of rat, mouse and boar.

Rights

In Copyright. URI: http://rightsstatements.org/vocab/InC/1.0/ This Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s).

DOI

10.25777/3jt7-2k07

Download

Share

COinS