ODF1 is one of the main sperm protein positive to monobromobimane and it is also recognized in other tissues.

CABRILLANA MARÍA EUGENIA; MONCLUS MARÍA DE LOS ÁNGELES; VINCENTI AMANDA EDITH; FORNÉS MIGUEL WALTER; YUNES ROBERTO

Ciudad de La Punta, SL

Congreso; XXVII Reunión Científica Anual de la Sociedad de Biología de Cuyo.; 2009

Sociedad de Biología de Cuyo

Mammalian spermatozoa undergo maturational changes as they pass through the epididymis, like the oxidation of thiols groups (S-H) to disulfides bonds (S-S). Disulfides are involved in sperm chromatin condensation and tail organelles stabilization. Our objective was determinate witch specific protein was involved in this process. In this work, we used the fluorescent thiol labeling agent monobromobimane (mBBr) to determine the thiol status in rat sperm head and tails during maturation. In electrophoretic pattern one major band, near to 27 kDa possesses high affinity to mBBr but the origin was unclear. To address the origin of proteins labeled by mBBr, sperm cells were fractionated and pure cell fractions verified by electron microscopy were analyzed by combination of SDS-PAGE and mBBr affinity properties. The major band comes from pure sperm tail fraction. Finally by MALDI-TOF techniques, this protein band was analyzed and the sequence highly correlated with ODF 1 data base. The results taken together demonstrate that ODF1 is one of the major protein bands contributing to mBBr fluorescence sperm tail pattern, detectable at light microscopy and SDS-PAGE. Now by inmuno techniques in several tissues we are looking for another protein/s detected by the correspondent antibody.