Changes in the protein composition of rat spermatozoa during maturation in the epididymis.
Spermatozoa from the testis and cauda epididymidis were solubilized by detergent treatment and electrophoresis on SDS polyacrylamide gels revealed that the relative amounts of 13 detergent-extractable proteins decreased during passage of spermatozoa through the epididymis, 6 increased, whilst the remainder showed little or no change. Lactoperoxidase-catalysed iodination of plasma membrane proteins showed that the components carrying most of the label in testicular spermatozoa had Mr values of 110 000, 94 000, 84 000, 55 000 and 42 000 whereas on cauda epididymal spermatozoa the Mr values were 47 000, 24 000, 17 000, 14 500 and 13 500. Substantial differences were also noted in the protein composition of rete testis fluid and cauda epididymal plasma. The results support the concept that there is a considerable reorganization of the molecular architecture of the plasma membrane of spermatozoa during maturation in the epididymis.
D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D004822:Epididymis; D007457:Iodine Radioisotopes; D007784:Lactoperoxidase; D008297:Male; D008565:Membrane Proteins / Q000378:metabolism*; D008970:Molecular Weight; D051381:Rats; D011919:Rats, Inbred Strains; D013079:Sperm Maturation; D013094:Spermatozoa / Q000378:metabolism*; D013737:Testis
D007457:Iodine Radioisotopes; D008565:Membrane Proteins; D007784:Lactoperoxidase