Effect of Gossypol on Boar Spermatozoal Adenosine Triphosphate Metabolism

References

• Acott T. S., Hoskins D. D. Bovine sperm forward motility protein. J Biol Chem 1978; 253: 6744–6750
   PubMed Web of Science ®Google Scholar
• Adam D. E., Wei J. Mass transport of ATP within the motile sperm. J Theor Biol 1975; 49: 125–145
   PubMed Web of Science ®Google Scholar
• Bonting S. L., Caravaggio L. L., Hawkins N. M. Studies on sodium-potassium-activated adenosinetriphosphatase. IV. Correlation with cation transport sensitive to cardiac glycosides. Archs Biochem Biophys 1962; 98: 414–419
   Web of Science ®Google Scholar
• Bonting S. L., Caravaggio L. L. Studies on sodium-potassium-activated adenosinetriphosphatase. V. Correlation of enzyme activity with cation flux in six tissues. Archs Biochem Biophys 1963; 101: 37–46
   PubMed Web of Science ®Google Scholar
• Brooks D. E. Examination of bull semen and of the bull and rabbit testis for the presence of creatine phosphate and arginine phosphate. J Reprod Fertil 1971; 26: 275–278
   PubMedGoogle Scholar
• Deluca M., Wannlund J., McElroy W. D. Factors affecting the kinetics of light emission from crude and purified firefly luciferase. Anal Biochem 1979; 95: 194–198
   PubMed Web of Science ®Google Scholar
• Dop C. V., Hutson S. M., Lardy H. A. Pyruvate metabolism in bovine epididymal spermatozoa. J Biol Chem 1977; 252: 1303–1308
   PubMed Web of Science ®Google Scholar
• Dunham E. T., Glynn I. M. Adenosinetri-phosphatase activity and the active movements of alkali metal ions. J Physiol Lond 1961; 156: 274–293
   Google Scholar
• Fawcett D. W. The structure of the spermatozoon. Frontiers in Reproduction and Fertility Control, R. O. Creep, M. A. Koblinsky. The MIT Press, Cambridge 1977; 353–378
   Google Scholar
• Fiske C. H., Subbarrow Y. The colorimetric determination of phosphorus. J Biol Chem 1925; 66: 375–400
   Google Scholar
• Ford W. C. L., Harrison A., Takkar G. L., Waites G. M. H. Inhibition of glucose catabolism in rat, hamster, rhesus monkey and human spermatozoa by α-chlorohydrin. Internat J Androl 1979; 2: 275–288
   Google Scholar
• Forrester I. T., Bradley M. P. Identification of calmodulin-like activity in human seminal plasma. Biochem Biophys Res Commun 1980; 92: 994–1001
   PubMed Web of Science ®Google Scholar
• Gibbons I. R. Studies on the protein components of cilia from tetrahymena pyriformis. Proc Natl Acad Sci USA 1963; 50: 1002–1010
   PubMed Web of Science ®Google Scholar
• Gibbons I. R. Sperm motility. Frontiers in Reproduction and Fertility Control, R. O. Greep, M. A. Koblinsky. The MIT Press, Cambridge 1977; 452–457
   Google Scholar
• Gibbons B. H., Gibbons I. R. Flagellar movement and adenosine triphosphatase activity in sea urchin sperm extracted with Triton X-100. J Cell Biol 1972; 54: 75–97
   PubMed Web of Science ®Google Scholar
• Gibbons I. R., Rowe A. J. Dynein: a protein with ATPase activity from cilia. Science 1965; 149: 424–426
   PubMed Web of Science ®Google Scholar
• Gov M. F., Springer M. S., Adler J. Sensory transduction in Escherichia coli: role of a protein methylation reaction in sensory adaptation. Proc Natl Acad Sci USA 1977; 74: 4964–4968
   PubMed Web of Science ®Google Scholar
• Gutmann I., Wahlefeld A. W. L-(+)-lactate determination with lactate dehydrogenase and NAD. Methods of Enzymatic Analysis2nd ed., H. U. Bergmeyer. Academic, New York 1974; Vol 2: 1464–1468
   Google Scholar
• Harrison R. A. P. The metabolism of mammalian spermatozoa. Frontiers in Reproduction and Fertility Control, R. O. Greep, M. A. Koblinsky. MIT Press, Cambridge 1977; 379–401
   Google Scholar
• Hunter F. E. Coupling of phosphorylation with oxidation. Methods in Enzymology, S. P. Colowick, N. Kaplan. Academic, New York 1955; Vol II: 610–616
   Google Scholar
• Jørgensen P. L. Isolation of (Na+ + K+)-ATPase. Methods in Enzymology, S. Fleischer, L. Packer. Academic, New York 1974; Vol XXXII: 277–290
   Google Scholar
• Lang G., Michal G. d-glucose 6-phosphate and d-fructose 6-phosphate. Methods of Enzymatic Analysis2nd ed., H. U. Bergmeyer. Academic, New York 1974; Vol 2: 1238–1242
   Google Scholar
• Mitani M., Koenuma M., Otake N. Studies on the ionophorous antibiotics. XII. Effects of ionophore lysocellin on cation distribution and respiration in mitochondria. J Antibiol 1977; 30: 829–835
   PubMed Web of Science ®Google Scholar
• Morton B. E., Lardy H. A. Cellular oxidative phosphorylation. I. Measurement in intact spermatozoa and other cells. Biochemistry 1967; 6: 43–49
   PubMed Web of Science ®Google Scholar
• Myers B. D., Throneberry G. O. Effect of gossypol on some oxidative respiratory enzymes. Plant Physiol 1966; 41: 787–791
   PubMed Web of Science ®Google Scholar
• Nevo A. C., Rikmenspoel R. Diffusion of ATP in sperm flagella. J Theor Biol 1970; 26: 11–18
   PubMed Web of Science ®Google Scholar
• Post R. L., Merritt C. R., Kingsolving C. R., Albright C. D. Membrane adenosine triphosphatase as a participant in the active transport of sodium and potassium in the human erythrocyte. J Biol Chem 1960; 235: 1796–1802
   PubMed Web of Science ®Google Scholar
• Post R. L., Sen A. K. Sodium and potassium-stimulated ATPase. Methods in Enzymology, R. W. Estabrook, M. E. Pullman. Academic, New York 1967; Vol X: 762–768
   Google Scholar
• Quinn P. J., White I. G., Wirrick B. R. Studies of the distribution of the major cations in semen and male accessory secretions. J Reprod Fertil 1965; 10: 379–388
   PubMedGoogle Scholar
• Quinn P. J., White I. G. Active cation transport in dog spermatozoa. Biochem J 1967; 104: 328–331
   PubMed Web of Science ®Google Scholar
• Quinn P. J., White I. G. The transport of cations by ram and bull spermatozoa. Aust J Biol Sci 1968; 21: 781–782
   PubMedGoogle Scholar
• Sherris D., Parkinson J. S. Posttranslational processing of methyl-accepting chemotaxis proteins in Escherichia coli. Proc Natl Acad Sci USA 1981; 78: 6051–6055
   PubMed Web of Science ®Google Scholar
• Slater E. C. Application of inhibitors and uncouplers for a study of oxidative phosphorylation. Methods in Enzymology, R. W. Estabrook, M. E. Pullman. Academic, New York 1967; Vol X: 48–57
   Google Scholar
• Strehler B. L. Adenosine-5′-triphosphate and creatine phosphate, determination with luciferase. Methods of Enzymatic Analysis2nd ed., H. U. Bergmeyer. Academic, New York 1974; Vol 4: 2112–2126
   Google Scholar
• Suter D., Chow D. Y. W., Martin I. C. A. Maintenance of motility in human spermatozoa by energy derived through oxidative phosphorylation and addition of albumin. Biol Reprod 1979; 20: 505–510
   PubMed Web of Science ®Google Scholar
• Tso W. W., Lee W. M. Seminal plasma and progressive motility of boar spermatozoa. Int J Androl 1980; 3: 243–250
   PubMedGoogle Scholar
• Tso W. W., Lee C. S. Variations of gossypol sensitivity in boar spermatozoal electron transport chain segments. Contraception 1981; 24: 569–576
   PubMed Web of Science ®Google Scholar
• Tso W. W., Lee C. S. Effect of gossypol on boar spermatozoa in vitro. Arch Androl 1981; 7: 85–88
   PubMed Web of Science ®Google Scholar
• Tso W. W., Lee C. S. Cottonseed oil as a vaginal contraceptive. Arch Androl 1982; 8: 11–14
   PubMed Web of Science ®Google Scholar
• Tso W. W., Lee W. M., Tsui K. C., Lam Y. F., Tso M. Y. W. Assay of progressive motion of boar spermatozoa. Arch Androl 1980; 4: 315–327
   PubMed Web of Science ®Google Scholar