Biomaterial Database

Sperm glycosidase as a plausible mediator of sperm binding to the vitelline envelope in Ascidians. 1986

M Hoshi

In the Ascidian, Ciona intestinalis, sperm alpha-L-fucosidase is concluded to be a recognition protein for the sperm receptor in the vitelline envelope. The spermatozoa bind to the vitelline envelope probably by forming rather stable substrate (alpha-L-fucoside)-enzyme complex at many spots. Experimental evidence indicates a good correspondence in the properties between receptor binding activity and alpha-L-fucosidase activity such as the effects of saccharides, of pH and of monoclonal antibodies raised against sperm alpha-L-fucosidase, and locus in the sperm. A general mechanism involving an enzyme as a recognition protein for the cell to cell binding is also discussed in relation to the molecular evolution of the recognition proteins.

UI	MeSH Term	Description	Entries
D008297	Male		Males
D005260	Female		Females
D005644	alpha-L-Fucosidase	An enzyme that catalyzes the hydrolysis of an alpha L-fucoside to yield an alcohol and L-fucose. Deficiency of this enzyme can cause FUCOSIDOSIS. EC 3.2.1.51.	Fucosidase,alpha-Fucosidase,alpha Fucosidase,alpha L Fucosidase
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D000911	Antibodies, Monoclonal	Antibodies produced by a single clone of cells.	Monoclonal Antibodies,Monoclonal Antibody,Antibody, Monoclonal
D001665	Binding Sites	The parts of a macromolecule that directly participate in its specific combination with another molecule.	Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D013084	Sperm-Ovum Interactions	Interactive processes between the oocyte (OVUM) and the sperm (SPERMATOZOA) including sperm adhesion, ACROSOME REACTION, sperm penetration of the ZONA PELLUCIDA, and events leading to FERTILIZATION.	Ovum-Sperm Interactions,Sperm Penetration,Egg-Sperm Interactions,Gamete Interactions,Oocyte-Sperm Interactions,Sperm-Egg Interactions,Sperm-Egg Penetration,Sperm-Oocyte Interactions,Sperm-Oocyte Penetration,Sperm-Ovum Penetration,Sperm-Zona Pellucida Penetration,Egg Sperm Interactions,Egg-Sperm Interaction,Gamete Interaction,Oocyte Sperm Interactions,Oocyte-Sperm Interaction,Ovum Sperm Interactions,Ovum-Sperm Interaction,Sperm Egg Interactions,Sperm Egg Penetration,Sperm Oocyte Interactions,Sperm Oocyte Penetration,Sperm Ovum Interactions,Sperm Ovum Penetration,Sperm Penetrations,Sperm Zona Pellucida Penetration,Sperm-Egg Interaction,Sperm-Egg Penetrations,Sperm-Oocyte Interaction,Sperm-Oocyte Penetrations,Sperm-Ovum Interaction,Sperm-Ovum Penetrations,Sperm-Zona Pellucida Penetrations
D013094	Spermatozoa	Mature male germ cells derived from SPERMATIDS. As spermatids move toward the lumen of the SEMINIFEROUS TUBULES, they undergo extensive structural changes including the loss of cytoplasm, condensation of CHROMATIN into the SPERM HEAD, formation of the ACROSOME cap, the SPERM MIDPIECE and the SPERM TAIL that provides motility.	Sperm,Spermatozoon,X-Bearing Sperm,X-Chromosome-Bearing Sperm,Y-Bearing Sperm,Y-Chromosome-Bearing Sperm,Sperm, X-Bearing,Sperm, X-Chromosome-Bearing,Sperm, Y-Bearing,Sperm, Y-Chromosome-Bearing,Sperms, X-Bearing,Sperms, X-Chromosome-Bearing,Sperms, Y-Bearing,Sperms, Y-Chromosome-Bearing,X Bearing Sperm,X Chromosome Bearing Sperm,X-Bearing Sperms,X-Chromosome-Bearing Sperms,Y Bearing Sperm,Y Chromosome Bearing Sperm,Y-Bearing Sperms,Y-Chromosome-Bearing Sperms
D014561	Urochordata	A subphylum of chordates intermediate between the invertebrates and the true vertebrates. It includes the Ascidians.	Ascidia,Tunicata,Ascidiacea,Ascidians,Sea Squirts,Tunicates,Urochordates,Ascidian,Sea Squirt,Squirt, Sea,Tunicate,Urochordate
D014817	Vitelline Membrane	The plasma membrane of the egg.	Membrane, Vitelline,Membranes, Vitelline,Vitelline Membranes