Purification of proteins from rat sperm membranes that interact with ligands other than phosphomannosyl residues.
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.
Belmonte
S
S
Instituto de Histología y Embriología, Facultad de Ciencias Médicas, Universidad Nacional de Cuyo, Argentina.
Sartor
T
T
Bertini
F
F
Sosa
M A
MA
D000818:Animals; D001826:Body Fluids / Q000737:chemistry; D002462:Cell Membrane / Q000737:chemistry*; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D004822:Epididymis / Q000378:metabolism; D005636:Fructosephosphates / Q000737:chemistry; D015151:Immunoblotting; D008297:Male; D008565:Membrane Proteins / Q000302:isolation & purification*; D008970:Molecular Weight; D051381:Rats; D017527:Receptor, IGF Type 2 / Q000737:chemistry; D012995:Solubility; D013094:Spermatozoa / Q000648:ultrastructure*
D005636:Fructosephosphates; D008565:Membrane Proteins; D017527:Receptor, IGF Type 2; C027618:fructose-6-phosphate