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Biology of Reproduction, Vol 29, 725-732, Copyright © 1983 by Society for the Study of Reproduction

ARTICLES

A bovine seminal plasma inhibitor of actin-stimulated myosin adenosine triphosphatase

TM Tamblyn

During attempts to isolate bovine sperm actin, persistent low molecular weight proteinaceous (LMWP) contaminants were found. A LMWP fraction was prepared by gel filtration chromatography on Sephadex G150. The LMWP was found in extracts of washed bovine ejaculated spermatozoa and in clarified bovine seminal plasma. It was substantially reduced in amount in bovine epididymal spermatozoa, indicating that it originated from secondary sex gland secretions. The LMWP inhibited rabbit muscle actin-stimulated myosin adenosine triphosphatase (actin-myosin ATPase) activity. The LMWP:actin ratio for 50% inhibition of actin-myosin ATPase was 2.6 +/- 0.12 mg LMWP per mg actin. The LMWP interfered with actin inhibition of deoxyribonuclease, indicating that LMWP interacted with actin. The LMWP from seminal plasma had an estimated molecular weight of 8300 and consisted of several acidic components. It had negligible protease activity and its inhibition of actin-myosin ATPase was independent of divalent cations. The LMWP appears to readily aggregate with itself and other proteins, which may be related to its physiological role in semen.


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S. Sanchez-Luengo, G. Aumuller, M. Albrecht, P. C. Sen, K. Rohm, and B. Wilhelm
Interaction of PDC-109, the Major Secretory Protein From Bull Seminal Vesicles, With Bovine Sperm Membrane Ca2+-ATPase
J Androl, March 1, 2004; 25(2): 234 - 244.
[Abstract] [Full Text] [PDF]


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Copyright © 1983 by the Society for the Study of Reproduction.