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Abstract
The ability of various synthetic peptide analogs of. Formyl-Met-Leu-Phe to induce chemotaxis in bull sperm is compared using an inverted capillary assay. The formyl group is essential for chemotactic activity and corresponding t-butyloxycarbonyl tripeptides are inactive. Sequence analogs, Formyl-Met-Phe-Leu, Formyl-Leu-Met-Phe and Formyl-Leu-Phe-Met are active. Replacement of Met and Leu by Pro does not diminish activity. Formyl-Met-Leu-Phe-NH2 is active suggesting that electrostatic interactions involving the carboxyl group may be unimportant in receptor interactions. The studies establish the importance of an amino terminal formyl group and a sequence of at least three hydrophobic residues, for inducing sperm chemotaxis.
Item Type: | Journal Article |
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Publication: | Biochemical and Biophysical Research Communications |
Publisher: | Elsevier science |
Additional Information: | Copyright of this article belongs to Elsevier science. |
Department/Centre: | Division of Biological Sciences > Molecular Biophysics Unit |
Date Deposited: | 05 Feb 2010 08:35 |
Last Modified: | 19 Sep 2010 05:35 |
URI: | http://eprints.iisc.ac.in/id/eprint/21096 |
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