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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1983-12-17
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pubmed:abstractText |
Fab fragments against 225 000 D glycoprotein (225 K), 87 000 D protein (87K) 80 000 D glycoprotein (80 K) of partially purified sperm-binding factor of Anthocidaris crassispina were prepared, and their effects upon fertilizability of dejellied homologous and heterologous eggs examined. Only the 225 K Fab impaired the fertilizability of homologous, not heterologous eggs by decreasing their sperm-binding capacity. It was concluded that 225 K glycoprotein is the active core structure of the sperm-binding factor of this species. The possible participation of the other two proteins as residual ingredients of the sperm-binding factor was also discussed. Immunofluorescence studies showed that 225 K core protein is localized on the whole surface of unfertilized eggs and of fully-grown oocytes. The fluorescence disappeared following fertilization.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0014-4827
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
148
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
243-8
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pubmed:dateRevised |
2003-11-14
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pubmed:meshHeading |
pubmed-meshheading:6354734-Animals,
pubmed-meshheading:6354734-Female,
pubmed-meshheading:6354734-Fluorescent Antibody Technique,
pubmed-meshheading:6354734-Glycoproteins,
pubmed-meshheading:6354734-Male,
pubmed-meshheading:6354734-Molecular Weight,
pubmed-meshheading:6354734-Ovum,
pubmed-meshheading:6354734-Protein Binding,
pubmed-meshheading:6354734-Sea Urchins,
pubmed-meshheading:6354734-Spermatozoa,
pubmed-meshheading:6354734-Zygote
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pubmed:year |
1983
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pubmed:articleTitle |
A 225 K dalton glycoprotein is the active core structure of the sperm-binding factor of the sea urchin, Anthocidaris crassispina.
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pubmed:publicationType |
Journal Article
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