An angiotensin-converting enzyme-inhibitory metabolite with partial structure of microginin in a cyanobacterium Anabaena fertilissima CCC597, producing fibrinolytic protease

Bagchi Suvendra Nath; Sondhia Shobha; Agrawal Manish Kumar<sup>*</sup>; Banerjee Sonali

doi:10.1007/s10811-015-0541-5

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An angiotensin-converting enzyme-inhibitory metabolite with partial structure of microginin in a cyanobacterium Anabaena fertilissima CCC597, producing fibrinolytic protease

作者：Bagchi Suvendra Nath; Sondhia Shobha; Agrawal Manish Kumar^*; Banerjee Sonali

来源：Journal of Applied Phycology, 2016, 28(1): 177-180.

DOI：10.1007/s10811-015-0541-5

摘要

Whole cell matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) of Anabaena fertilissima CCC597 revealed the presence of a microginin (M (r) = 565 Da), which was purified using ODS C18 solid-phase extraction followed by quaternary methyl ammonium (QMA)-ion exchange and reverse-phase liquid chromatography. Its partial structure was deduced upon LC-MS/MS as beta-amino-alpha-hydroxy-decanoic acid-Ala-MeLeu-Tyr. Microginin-565 inhibited rabbit angiotensin-converting enzyme activity at an apparent IC50 = 9.8 mu M.