@article{tubbs_hall_scott_clark_hermon_bazemore-walker_2002, title={Binding of protein D/E to the surface of rat epididymal sperm before ejaculation and after deposition in the female reproductive tract}, volume={23}, number={4}, journal={Journal of Andrology}, author={Tubbs, C. E. and Hall, J. C. and Scott, R. and Clark, V. P. and Hermon, T. L. and Bazemore-Walker, C.}, year={2002}, pages={512–521} }
 @article{hall_tubbs_1998, title={Quantification of epididymal retinoic acid-binding protein (ERABP) mRNA in different anatomical regions of the adult rat epididymis}, volume={42}, number={4}, journal={Biochemistry and Molecular Biology International}, author={Hall, J. C and Tubbs, C. E.}, year={1998}, pages={833–841} }
 @article{hall_tubbs_1997, title={Purification and characterization of protein D/E, a putative sperm-binding protein involved in fertilization}, volume={27}, ISSN={["1082-6068"]}, DOI={10.1080/10826069708001282}, abstractNote={We describe a method for the efficient purification of a 32 Kd glycoprotein from rat epididymal tissue. The glycoprotein was purified by gel filtration, ion-exchange, affinity, and reverse phase high pressure liquid chromatography. The highly purified glycoprotein was radiolabeled with an iodinatable, cleavable, photoreactive cross-linking agent, 1-[N-(2-hydrox-5-azidobenzoyl)-2-aminoethyl]-4-(-hydroxysuccini mid yl)-succinate (HAHS). The soluble radiolabeled glycoprotein was bound to washed epididymal spermatozoa in a time-dependent, saturable, and reversible manner. Scatchard analysis demonstrates that there are approximately 3,403 binding sites/spermatozoon. The binding efficiency (Kd) for spermatozoa was approximately 2.0 x 10(-10) M. The function of this glycoprotein was verified by using an in vivo artificial insemination fertilization assay. The fertility rate for control spermatozoa was approximately 53%, but the rate for spermatozoa exposed to polyclonal anti-glycoprotein antibodies was only 5%. These data suggest that the binding of the glycoprotein to the surface of rat spermatozoa is mediated by a receptor-type mechanism and is involved in the fertilization process.}, number={4}, journal={PREPARATIVE BIOCHEMISTRY & BIOTECHNOLOGY}, author={Hall, JC and Tubbs, CE}, year={1997}, pages={239–251} }
 @article{hall_jacobetz_lamarche_kochins_tubbs_1997, title={Purification, characterization, and expression of rat epididymal beta-D-galactosidase}, volume={42}, number={3}, journal={Biochemistry and Molecular Biology International}, author={Hall, J. C. and Jacobetz, D. R. and LaMarche, M. D. and Kochins, J. G. and Tubbs, C. E.}, year={1997}, pages={443–451} }