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Int J Biochem Cell Biol. 1995 Jun;27(6):603-11.

Human seminal plasma beta-microseminoprotein: its purification, characterization, and immunohistochemical localization.

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  • 1Department of Medical Biochemistry, Shiga University of Medical Science, Otsu, Japan.


beta-Microseminoprotein was very efficiently purified from human seminal plasma with only three steps including DEAE-Sephacel and Zinc-chelate Sepharose CL-6B column chromatography. The purified protein was a non-glycoprotein with a molecular weight (M(r)) of 19,000 and 17,000 on gel filtration and reduced SDS-PAGE, respectively. The protein gave six bands from M(r) 15,600 to 25,500 on non-reduced SDS-PAGE. The characterization including the molecular weight, amino acid sequence of N-terminus and concentrations in various body fluids is discussed. Furthermore, the immunohistochemical localization of the protein among various human tissues is demonstrated.

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