A Nonglycosylated, 68-kDa α-l-Fucosidase Is Bound to the Mollusc BivalveUnio elongatulusSperm Plasma Membrane and Differs from a Glycosylated 56-kDa Form Present in the Seminal Fluid-Reference-Cited by-同舟云学术

A Nonglycosylated, 68-kDa α-l-Fucosidase Is Bound to the Mollusc BivalveUnio elongatulusSperm Plasma Membrane and Differs from a Glycosylated 56-kDa Form Present in the Seminal Fluid

Published:1997-05 Issue:1 Volume:234 Page:54-58
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Focarelli R.,Cacace M.G.,Seraglia R.,Rosati F.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference23 articles.

1. GENETIC DEFECTS IN GLYCOPROTEIN METABOLISM

2. M. Hoshi, R. De Santis, M. R. Pinto, F. Cotelli, F. Rosati, 1982, The Sperm Cell, 107, 110, The Hague, NL, Nijhoff

3. Immunocytochemical localization and biochemical characterization of a novel plasma membrane-associated, neutral pH optimum α-l-fucosidase from rat testis and epididymal spermatozoa

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