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Three new components contained in the vitelline coat of Tegula pfeifferi

Published online by Cambridge University Press:  16 July 2018

Kazu Haino-Fukushima
Affiliation:
Life Science Institute, Sophia University, Chiyoda-ku, Tokyo 102-8554, Japan
Xuxi Fan
Affiliation:
Department of Biology, Tokyo Metropolitan University, Hachioji, Tokyo 192-0397, Japan
Shouka Nakamura
Affiliation:
Department of Biology, Tokyo Metropolitan University, Hachioji, Tokyo 192-0397, Japan

Extract

The vitelline coat (VC) lysin of Tegula, a marine molluscan genus, is released from the acrosome of sperm during fertilisation and can lyse the VC of only the same species. The lytic action of this lysin against the VC is not an enzymatic reaction, but a stoichiometric and irreversible one (Haino-Fukushima, 1974).

The VC of Tegula pfeifferi consists of glycoproteins containing sulphated polysaccharides, which account for roughly two-thirds of the entire weight of the VC. The presence of a large quantity of polysaccharides in the VC had prevented rapid progress in the analysis of its protein components. Last year, we succeeded in a complete solubilisation of the VC by boiling for a long time in 1% SDS solution, and determined the cDNA sequence coding for a mature 41 kDa glycoprotein, which appears to be the major component of the VC from the results of SDS-polyacrylamide gel electrophoresis (PAGE). The cDNA, referred to as vcp41, comprises 1072 base pairs and contains one open reading frame with a sequence for 319 amino acids containing 19 amino acids of a signal peptide. The deduced amino acid sequence has five N-glycosylation sites and ten cysteine residues. It seems that almost 7 kDa in this 41kDa glycoprotein is polysaccharide constituents (Fan & Haino-Fukushima, 1998).

Type
Special Lecture for Citizens
Copyright
Copyright © Cambridge University Press 1999

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References

Fan, X. & Haino-Fukushima, K. (1998). Zool. Sci. 15 (abstract).Google Scholar
Haino-Fukushima, K. (1974). Biochim. Biophys. Acta 352, 179–91.CrossRefGoogle Scholar