Fawell, S. E., Pappin, D. J., McDonald, C. J., Higgins, S. J. (May 1986) Androgen-regulated proteins of rat seminal vesicle secretion constitute a structurally related family present in the copulatory plug. Mol Cell Endocrinol, 45 (2-3). pp. 205-13. ISSN 0303-7207 (Print)0303-7207 (Linking)
Abstract
All the major androgen-regulated secretory proteins of rat seminal vesicles have been purified in high yield from polyacrylamide gels using electroelution. In the process a sixth previously undocumented protein has been identified. Amino acid compositions of all the proteins are very similar and highly unusual, being high in lysine and arginine, and with 40-50% of the residues accounted for by serine, glycine and glutamate/glutamine. N-Terminal amino acid sequences for 3 of the proteins show that they are clearly the products of related genes. At least one of the other proteins is N-terminally blocked in vivo. Antibodies specific for each protein have been raised and provide evidence of structural similarity between the proteins. The antibodies were also used in immunofluorescence histochemistry with the rat copulatory plug, showing for the first time that all the major proteins of seminal vesicle secretion are components of this reproductive structure.
Item Type: | Paper |
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Uncontrolled Keywords: | Amino Acid Sequence Amino Acids/analysis Animals Copulation Electrophoresis, Polyacrylamide Gel Epitopes/immunology Fluorescent Antibody Technique Histocytochemistry Immune Sera/immunology Male Proteins/ analysis/immunology/physiology Rats Rats, Inbred Strains Seminal Vesicles/ secretion |
Subjects: | bioinformatics > genomics and proteomics > design > amino acid design bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification |
CSHL Authors: | |
Communities: | CSHL labs > Pappin lab |
Depositing User: | Matt Covey |
Date: | May 1986 |
Date Deposited: | 18 Sep 2014 20:25 |
Last Modified: | 18 Sep 2014 20:25 |
Related URLs: | |
URI: | https://repository.cshl.edu/id/eprint/30742 |
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