Partial structures and binding studies of maitotoxin, the most potent marine toxin.

M. Murata; M. Sasaki; A. Yokoyama; T. Iwashita; F. Gusovsky; J. W. Daly; T. Yasumoto

Partial structures and binding studies of maitotoxin, the most potent marine toxin.

M. Murata, M. Sasaki, A. Yokoyama, T. Iwashita, F. Gusovsky, J. W. Daly, T. Yasumoto

LIF - Molecular and Chemical Life Science

Tohoku University

Research output: Contribution to journal › Article › peer-review

8 Citations (Scopus)

Abstract

Partial structures of maitotoxin (MTX) were deduced by extensive two-dimensional NMR measurements, showing that the toxin had carbon-carbon double bonds in both termini of the molecule, and a primary alcohol group at the end. These functionalities were used for preparation of a radioligand of MTX; [3H]H-MTX and [3H]benzoyl-MTX. Both radioligands had high levels of non-specific binding to tissues. The binding of [3H]MTX to rat glioma C6 cells was inhibited by a didesulfo-MTX, suggesting the presence of the specific site for MTX-binding on the external surface of the cell membrane.

Original language	English
Pages (from-to)	470-473
Number of pages	4
Journal	Bulletin de la Société de pathologie exotique (1990)
Volume	85
Issue number	5 Pt 2
Publication status	Published - 1992

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T1 - Partial structures and binding studies of maitotoxin, the most potent marine toxin.

AU - Murata, M.

AU - Sasaki, M.

AU - Yokoyama, A.

AU - Iwashita, T.

AU - Gusovsky, F.

AU - Daly, J. W.

AU - Yasumoto, T.

PY - 1992

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N2 - Partial structures of maitotoxin (MTX) were deduced by extensive two-dimensional NMR measurements, showing that the toxin had carbon-carbon double bonds in both termini of the molecule, and a primary alcohol group at the end. These functionalities were used for preparation of a radioligand of MTX; [3H]H-MTX and [3H]benzoyl-MTX. Both radioligands had high levels of non-specific binding to tissues. The binding of [3H]MTX to rat glioma C6 cells was inhibited by a didesulfo-MTX, suggesting the presence of the specific site for MTX-binding on the external surface of the cell membrane.

AB - Partial structures of maitotoxin (MTX) were deduced by extensive two-dimensional NMR measurements, showing that the toxin had carbon-carbon double bonds in both termini of the molecule, and a primary alcohol group at the end. These functionalities were used for preparation of a radioligand of MTX; [3H]H-MTX and [3H]benzoyl-MTX. Both radioligands had high levels of non-specific binding to tissues. The binding of [3H]MTX to rat glioma C6 cells was inhibited by a didesulfo-MTX, suggesting the presence of the specific site for MTX-binding on the external surface of the cell membrane.

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JF - Bulletin de la Société de pathologie exotique (1990)

IS - 5 Pt 2

ER -

Partial structures and binding studies of maitotoxin, the most potent marine toxin.

Abstract

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