Studies on the egg-membrane lysin of Tegula pfeifferi: Isolation and chemical analysis of the egg membrane

Haino, K.; Kigawa, M.

doi:10.1016/0014-4827(66)90274-6

Cited by 16 publications

(11 citation statements)

References 23 publications

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“…This is supported by the fact that the natural substrate for the three lysins, the egg-membrane of Megathura crenuluta, contains a glycoprotein (E. Heller and M. A. Raftery, unpublished results) as does the egg membrane of Trgulu pfeifferi (Haino and Kigawa, 1966). In this way the egg-membrane lysins would tend to bind more strongly to a carbohydrate resin like Sephadex G-75.…”

Section: Discussionmentioning

confidence: 96%

“…A comparison with the egg-membrane lysin of Tegula pfeifferi (Haino, 1971) shows that egg-membrane lysins A, B, and C of Meguthura crenulutu are different in some respects, such as molecular weight, PI, and amino acid composition. This species difference might support the view that the eggmembrane lysins are species specific.…”

Section: Discussionmentioning

confidence: 99%

“…Further studies on the Megathuru crenuluta egg-membrane lysin were done by Krauss (1950). Recently, an egg-membrane lysin having a molecular weight of 8800 has been isolated from a sperm extract of Tegulu pjeifferi (Haino, 1971). A similar enzyme, reported to be located in the acrosomes of mammalian spermatozoa, has been isolated (Stambaugh and Buckley, 1972;Zaneveld et a/., 1972) and it is thought that this enzyme dissolves a small tunnel in the zona pellucida through which the spermatozoon can penetrate the egg (Stambaugh and Buckley, 1972).…”

mentioning

confidence: 99%

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Isolation and purification of three egg-membrane lysins from sperm of marine invertebrate Megathura crenulata (giant keyhole limpet)

Heller¹,

Raftery²

1973

Biochemistry

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Three enzymes which lyse the egg-membrane of the marine invertebrate Megathura crenulata were obtained from the sperm of a single individual as well as from pooled samples of sperm from several males of the same species. The three enzymes ("lysins") were purified to homogeneity by a combination of gel filtration and ion-exchange chromatography. The three egg-membrane lysins were different as .judged by chromatographic behavior, gel electrophoresis

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Section: Discussionmentioning

confidence: 96%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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Isolation and purification of three egg-membrane lysins from sperm of marine invertebrate Megathura crenulata (giant keyhole limpet)

Heller¹,

Raftery²

1973

Biochemistry

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“…The VC of each species was isolated and purified according to a published procedure (Haino & Kigawa 1966). Isolated VC was suspended at 0.1% in a 0.5 M KCl solution containing a 0.03 M phosphate buffer (pH 7.8) and 1 m M ethylenediamine tetraacetic acid (EDTA; Haino & Kigawa 1969).…”

Section: Methodsmentioning

confidence: 99%

Vitelline‐coat lysin: Comparison of lysins among three species in the genus Tegula

1999

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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.

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“…The enzymatic nature of the lysin can be better under stood by examining the substrate upon which it acts. Haino and Kigawa (1966) have characterized the egg envelope of the gastropod Tegula pfeifferi which is dissolved by homologous sperm lysin. They have found that the substrate is a glycoprotein containing 33% protein, 16% galactosamine, 11%…”

Section: Sperm Substances Involved In Fertilizationmentioning

confidence: 99%

Gamete surface molecular components and their functional roles in sperm-egg interactions of the horseshoe crab, Limulus polyphemus L. (Merostomata): an immunological and biochemical approach

Mowbray

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Studies on the egg-membrane lysin of Tegula pfeifferi: Isolation and chemical analysis of the egg membrane

Cited by 16 publications

References 23 publications

Isolation and purification of three egg-membrane lysins from sperm of marine invertebrate Megathura crenulata (giant keyhole limpet)

Isolation and purification of three egg-membrane lysins from sperm of marine invertebrate Megathura crenulata (giant keyhole limpet)

Vitelline‐coat lysin: Comparison of lysins among three species in the genus Tegula

Gamete surface molecular components and their functional roles in sperm-egg interactions of the horseshoe crab, Limulus polyphemus L. (Merostomata): an immunological and biochemical approach

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