A nonglycosylated, 68-kDa alpha-L-fucosidase is bound to the mollusc bivalve Unio elongatulus sperm plasma membrane and differs from a glycosylated 56-kDa form present in the seminal fluid.

@article{Focarelli1997AN6,
  title={A nonglycosylated, 68-kDa alpha-L-fucosidase is bound to the mollusc bivalve Unio elongatulus sperm plasma membrane and differs from a glycosylated 56-kDa form present in the seminal fluid.},
  author={Riccardo Focarelli and Marcello G. Cacace and Roberta Seraglia and Floriana Rosati},
  journal={Biochemical and biophysical research communications},
  year={1997},
  volume={234 1},
  pages={
          54-8
        }
}
The male reproductive system of the mollusc bivalve Unio elongatulus contains two distinct forms of alpha-L-fucosidase, one present in the gonad fluid and a second one associated with the sperm plasma membrane. Both activities were purified to homogeneity. The soluble seminal plasma enzyme had an oligomeric MW of 56 kDa as determined by MALDI-TOF mass spectrometry, whereas the enzyme purified from sperm plasma membranes had an MW of 68 kDa. Analyzed by lectin blotting with ConA and PNA, the 68… CONTINUE READING

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