| Title: | The primary structure of aphrodisin |
| Author(s): | Henzel WJ; Rodriguez H; Singer AG; Stults JT; Macrides F; Agosta WC; Niall H; |
| Address: | "Department of Developmental Biology, Genentech, Inc., South San Francisco, California 94080" |
| ISSN/ISBN: | 0021-9258 (Print) 0021-9258 (Linking) |
| Abstract: | "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" |
| Keywords: | "Amino Acid Sequence Animals Chromatography, High Pressure Liquid Cricetinae Male Molecular Sequence Data Molecular Weight Peptide Mapping Pheromones Proteins/*analysis;" |
| Notes: | "MedlineHenzel, W J Rodriguez, H Singer, A G Stults, J T Macrides, F Agosta, W C Niall, H eng HD19764/HD/NICHD NIH HHS/ NS12344/NS/NINDS NIH HHS/ Research Support, U.S. Gov't, P.H.S. 1988/11/15 J Biol Chem. 1988 Nov 15; 263(32):16682-7" |
