Molecular Human Reproduction, Vol. 5, No. 9, 809-815,
September 1999
© 1999 European Society of Human Reproduction and Embryology
Regulation of sperm function |
Characterization of human semen 
-L-fucosidases
1 Department of Chemistry, 111 Research Drive, Lehigh University, and 2 Department of Biological Sciences, Lehigh University, Bethlehem, PA 18015, USA
Abstract
Human semen contains a large amount of 
-L-fucosidase activity, the great majority of which is found in the seminal fluid. Immunocytochemical studies indicate that a small amount of semen fucosidase activity is present on the sperm plasma membrane, primarily in the posterior head region. Subcellular fractionation studies also indicate that sperm -L-fucosidase is present in the plasma membrane-enriched fraction. Comparative characterization of human seminal fluid and sperm -L-fucosidases indicates that seminal fluid -L-fucosidase has a broad pH optimum curve with a number of near-equal maxima between pH 4.8 and 7.0 while sperm fucosidase has a major optimum between pH 3.4 and 4.0. Isoelectric focusing indicates that seminal fluid -L-fucosidase contains three to six isoforms with isoelectric points (pI) of 5–7 while sperm fucosidase contains two distinct isoforms with pI values of 5.2 ± 0.2 and 7.0 ± 0.2. Western blotting indicates that seminal fluid fucosidase contains a major protein band with a molecular mass ratio (Mr) of ~56 kDa while sperm fucosidase contains a major protein band of ~51 kDa. The overall results indicate the presence of a low-abundance, plasma membrane-associated human sperm -L-fucosidase, which is different in its properties from human seminal fluid -L-fucosidase(s), and whose function is not yet known.
-L-fucosidase/semen/seminal fluid/spermatozoa
Notes
3 To whom correspondence should be addressed
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