scholarly journals Complementary approach for analysis of phospholipids by liquid chromatography hyphenated to elemental and molecular mass spectrometry

Author(s):  
Christian Vosse ◽  
Georgina M. Thyssen ◽  
Michael Sperling ◽  
Uwe Karst ◽  
Heiko Hayen
2014 ◽  
Vol 1370 ◽  
pp. 40-49 ◽  
Author(s):  
Hanyong Peng ◽  
Bin Hu ◽  
Qingqing Liu ◽  
Zonglin Yang ◽  
Xiufen Lu ◽  
...  

1978 ◽  
Vol 14 (9) ◽  
pp. 699-702
Author(s):  
L. N. Sosulina ◽  
L. I. Nazarova ◽  
E. M. Nikonorov ◽  
T. G. Zubkevich

2014 ◽  
Vol 406 (24) ◽  
pp. 5853-5865 ◽  
Author(s):  
Miguel Ángel García-Sevillano ◽  
Tamara García-Barrera ◽  
Francisco Navarro ◽  
Jürgen Gailer ◽  
José Luiz Gómez-Ariza

2008 ◽  
Vol 23 (3) ◽  
pp. 378-384 ◽  
Author(s):  
Diego Esteban-Fernández ◽  
M. Montes-Bayón ◽  
E. Blanco González ◽  
M. M. Gómez Gómez ◽  
M. A. Palacios ◽  
...  

2020 ◽  
Vol 21 (17) ◽  
pp. 6389
Author(s):  
Hongmei Zeng ◽  
Jingjing Cai ◽  
Hidemi Hatabayashi ◽  
Hiroyuki Nakagawa ◽  
Hiromitsu Nakajima ◽  
...  

In the biosynthesis of aflatoxin, verA, ver-1, ordB, and hypA genes of the aflatoxin gene cluster are involved in the pathway from versicolorin A (VA) to demethylsterigmatocystin (DMST). We herein isolated each disruptant of these four genes to determine their functions in more detail. Disruptants of ver-1, ordB, and hypA genes commonly accumulated VA in their mycelia. In contrast, the verA gene disruptant accumulated a novel yellow fluorescent substance (which we named HAMA) in the mycelia as well as culture medium. Feeding HAMA to the other disruptants commonly caused the production of aflatoxins B1 (AFB1) and G1 (AFG1). These results indicate that HAMA pigment is a novel aflatoxin precursor which is involved at a certain step after those of ver-1, ordB, and hypA genes between VA and DMST. HAMA was found to be an unstable substance to easily convert to DMST and sterigmatin. A liquid chromatography-mass spectrometry (LC-MS) analysis showed that the molecular mass of HAMA was 374, and HAMA gave two close major peaks in the LC chromatogram in some LC conditions. We suggest that these peaks correspond to the two conformers of HAMA; one of them would be selectively bound on the substrate binding site of VerA enzyme and then converted to DMST. VerA enzyme may work as a key enzyme in the creation of the xanthone structure of DMST from HAMA.


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