Vitelline-coat lysin: comparison of lysins among three species in the genus Tegula.
Vitelline-coat lysins from two species of marine mollusc of the genus Tegula, Tegula lischkei and Tegula sp., were purified and their properties compared with those of Tegula pfeifferi. Cross-reaction tests among these three species proved that the lysin action on the vitelline coat was species specific. Each of the lysins from these three species is a single, basic polypeptide with a molecular weight of 16000-17000 and an isoelectric point of pH 10.5. All of them share a common antibody recognition site(s) for the anti-T. pfeifferi lysin antibody. Their amino acid sequences were analyzed using intact lysins and peptides separated by reverse phase high-performance liquid chromatography after V8 proteinase digestion. The amino acid sequences of the N-terminus (Nos 1-66) from the three species showed 98% homology, and those of the C-terminus (Nos 91-118) showed 89% homology. It was concluded that the species specificity of the vitelline coat lysin appears to be determined by a sequence of 24 residues (Nos 67-90) in the middle region of the molecule.
Haino-Fukushima
K
K
Department of Biology, Tokyo Metropolitan University, Hachiohji, Japan. haino-kazu@c.metro-u.ac.jp
Shimoirisa
M
M
Yamakawa
Y
Y
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism; D015151:Immunoblotting; D007525:Isoelectric Focusing; D008297:Male; D008969:Molecular Sequence Data; D008974:Mollusca / Q000201:enzymology / Q000502:physiology*; D009088:Mucoproteins / Q000737:chemistry* / Q000378:metabolism; D013045:Species Specificity; D013094:Spermatozoa / Q000378:metabolism; D014817:Vitelline Membrane / Q000737:chemistry* / Q000378:metabolism
D004798:Enzymes; D009088:Mucoproteins; C010393:lysin, gastropoda