The primary structure of aphrodisin

Aphrodisin is a protein which is secreted in hamster vaginal discharge and acts via the vomeronasal organ of the accessory olfactory system to elicit copulatory behavior in male hamsters. The complete primary structure of aphrodisin was determined by sequence analysis of intact aphrodisin after unbl...

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Bibliographic Details
Published in:The Journal of biological chemistry 1988-11, Vol.263 (32), p.16682-16687
Main Authors: Henzel, W J, Rodriguez, H, Singer, A G, Stults, J T, Macrides, F, Agosta, W C, Niall, H
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Aminoacids, peptides. Hormones. Neuropeptides
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Chromatography, High Pressure Liquid
Cricetinae
Fundamental and applied biological sciences. Psychology
Male
Molecular Sequence Data
Molecular Weight
Peptide Mapping
Pheromones
Proteins
Proteins - analysis
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Summary:Aphrodisin is a protein which is secreted in hamster vaginal discharge and acts via the vomeronasal organ of the accessory olfactory system to elicit copulatory behavior in male hamsters. The complete primary structure of aphrodisin was determined by sequence analysis of intact aphrodisin after unblocking the amino terminus with pyroglutamate aminopeptidase and from peptides generated by trypsin and Lys-C digests. Alignment of the peptides was obtained from sequence analysis of peptides from cyanogen bromide and hydroxylamine cleavages. The protein consists of 151 residues of Mr = 17,000. It has disulfide bonds linking cysteine residues at positions 38 and 42 and at 57 and 149. N-acetylglucosamine residues are linked to asparagines at positions 41 and 69. Based on its similarity to the major urinary proteins in rats and mice, aphrodisin is a putative member of the alpha 2u-globulin superfamily of extracellular proteins.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)37444-1