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Purification and immunocytochemical localization of the vitelline coat lysin of abalone spermatozoa
Affiliation:1. Department of Biology, Faculty of Science, Tokyo Metropolitan University, Fukasawa, Setagaya-ku, Tokyo 158, Japan;2. Department of Anatomy, Teikyo University School of Medicine, Kaga, Itabashi-ku, Tokyo 173, Japan;1. Department of Surgery, Division of Adult Cardiothoracic Surgery, University of California, San Francisco, and San Francisco Veterans Affairs Health Care System, USA;2. School of Medicine, University of California, San Francisco, USA;3. Department of Radiology and Biomedical Imaging, University of California, San Francisco, and San Francisco Veterans Affairs Health Care System, USA;1. Dr Hasan Sadikin Hospital, Indonesia;2. Riau University, Indonesia;1. Department of Zoology, University of Delhi, Delhi 110007, India;2. Center for Individualized Medicine, Mayo Clinic, 200 First Street SW, Rochester, MN, 55905, USA
Abstract:Spermatozoa of the abalone Haliotis discus were treated with high-calcium seawater to induce the acrosome reaction. The soluble components released from the sperm acrosomal vesicles showed potent lytic activity on the egg vitelline coat. A vitelline coat lysin was purified by salting-in, preparative polyacrylamide gel electrophoresis, and high-performance liquid chromatography. Its molecular weight was 15,500 and its isoelectric point 9.6. These properties were similar to those of other molluskan vitelline coat lysins. The lysin was immunocytochemically localized using a protein A-gold technique, in the posterior half of the acrosomal vesicle.
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