STRUCTURE OF THE CYCLO-HEPTAPEPTIDE IN MICROCYSTIN-LR DETERMINED BY NMR

Chinese Journal of Magnetic Resonance ›› 2000, Vol. 17 ›› Issue (1): 23-28.

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STRUCTURE OF THE CYCLO-HEPTAPEPTIDE IN MICROCYSTIN-LR DETERMINED BY NMR

ZHANG Tao¹, MAO Xi'an¹, HE Jiawan²

1 State Key Laboratory of Magnetic Resonance & Atomic and Molecular Physics, Wuhan Institute of Physics and Mathematics, The Chinese Academy of Sciences, Wuhan 430071;
2 Institute of Hydrobiology, The Chinese Academy of Sciences, Wuhan 430072

Received:1999-11-04 Revised:1999-11-30 Published:2000-02-05 Online:2018-01-10

Abstract

Abstract: A toxin isolated from waterbloom of the colonial cyanobacterium Microcystis aeruginosa collected in a fish pond was studied by one-dimensional and two-dimensional nuclear magnetic resonance techniques. Combined with other analytical techniques, it is shown that this toxin is just microcystin-LR, the most common cyclo-heptapeptide. The connectivity of amino acids in the cyclic part of this toxin is determined.

Key words: Microcystin-LR, NMR, Chemical shift, Amino acid connectivity

ZHANG Tao, MAO Xi'an, HE Jiawan. STRUCTURE OF THE CYCLO-HEPTAPEPTIDE IN MICROCYSTIN-LR DETERMINED BY NMR[J]. Chinese Journal of Magnetic Resonance, 2000, 17(1): 23-28.

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STRUCTURE OF THE CYCLO-HEPTAPEPTIDE IN MICROCYSTIN-LR DETERMINED BY NMR

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