A sperm-binding protein (SBP) was purified from the rat seminal vesicle fluid by salting out, gel filtration and ionic exchange chromatography. SBP migrates on polyacrylamide gel as single band in non-denaturing conditions, but as two bands in denaturing conditions. These two protein bands had the same electrophoretic mobility of the major seminal vesicle secretory proteins RSV-IV and RSV-V. Aminoacid composition analysis revealed that SBP is actually constituted by RSV-IV and RSV-V in a 1: 1 ratio. We conclude that the two secretory proteins form a complex in the seminal vesicle fluid.

Characterization of a sperm-coating antigen in rat.

SANSONE, GIOVANNI;ABRESCIA, PAOLO
1987

Abstract

A sperm-binding protein (SBP) was purified from the rat seminal vesicle fluid by salting out, gel filtration and ionic exchange chromatography. SBP migrates on polyacrylamide gel as single band in non-denaturing conditions, but as two bands in denaturing conditions. These two protein bands had the same electrophoretic mobility of the major seminal vesicle secretory proteins RSV-IV and RSV-V. Aminoacid composition analysis revealed that SBP is actually constituted by RSV-IV and RSV-V in a 1: 1 ratio. We conclude that the two secretory proteins form a complex in the seminal vesicle fluid.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/132124
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