Purification of proteins from rat sperm membranes that interact with ligands other than phosphomannosyl residues.

BELMONTE S; SARTOR T; BERTINI MF; SOSA MA

ANDROLOGIA

WILEY-BLACKWELL PUBLISHING, INC

Año: 2000 vol. 30 p. 115 - 118

0303-4569

Andrologia. 2000 Mar;32(2):115-8. Andrologia. 2000 Mar;32(2):115-8. Purification of proteins from rat sperm membranes that interact with ligands other than phosphomannosyl residues. Belmonte S, Sartor T, Bertini F, Sosa MA. Belmonte S, Sartor T, Bertini F, Sosa MA. Source Instituto de Histología y Embriología, Facultad de Ciencias Médicas, Universidad Nacional de Cuyo, Argentina. Abstract In this study proteins were purified from rat sperm membranes which might be the high affinity sites for ligands of epididymal fluid other than the mannose-6-phosphate receptors. The sperm membrane proteins were solubilized and passed over an affinity column containing epididymal fluid proteins coupled to a matrix. Two bands in the range of 45-55 kDa were eluted from the column with fructose-6-phosphate but not with mannose-6-phosphate. Although the molecular weight of these proteins are similar to those of the cation-dependent phosphomannosyl receptors they are not related. These two proteins may correspond either to two different receptors or to forms of the same receptor that recognize ligands from rat epididymal fluid. Sequencing and identification of these proteins will be the aim of future studies.