Surface Glycoprotein Changes in Ram Spermatozoa During Epididymal Maturation 1

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Abstract
Three radiolabeling procedures were applied to ram spermatozoa obtained at three different stages of posttesticular development: on leaving the testis (testicular sperm); after epididymal transit (cauda epididymal sperm); and after exposure to accessory sex gland secretions (ejaculated sperm). The washed spermatozoa were subjected to three radiolabeling treatments: 1) galactose oxidase and sodium boro [3H]hydride (galactosyl and galactosaminyl residues); 2) sodium metaperiodate and NaBH4 (sialyl residues); and 3) chloroglycoluril and Na125 I (tyrosyl residues). High resolution sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoretic analysis of the surface radiolabeling patterns confirms earlier studies in demonstrating an overall shift in the predominant labeled glycoproteins from the zone 78-115 kd in testicular spermatozoa to relatively low molecular weights of between 15 and 95 kd in cauda epididymal or ejaculated spermatozoa. Labeling procedures specific for glycoproteins and sialoglycoproteins revealed additional complexities in the surface transformation patterns of ram spermatozoa and suggest that cauda epididymal spermatozoa exposed to accessory sex gland secretions adsorb or produce a component of high molecular weight (approx. 350 kd).

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