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形式
powder
储存温度
−20°C
SMILES字符串
CN1c2cc(C)c(C)cc2N=C3C(=O)NC(=O)N=C13
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生化/生理作用
Lumiflavine (Lumiflavin) is produced by the photolysis of vitamin B2 (Riboflavin). Lumiflavine, a riboflavin uptake inhibitor, is used to study riboflavin uptake in intestinal epithelial (Caco-2) and other epithelial cells.
警示用语：
Warning
危险声明
危险分类
Muta. 2
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
Minako Kondo et al.
The journal of physical chemistry. B, 110(41), 20107-20110 (2006-10-13)
Ultrafast time-resolved infrared (TRIR) spectra of flavin adenine dinucleotide (FAD) and the anion of lumiflavin (Lf-) are described. Ground-state recovery and excited-state decay of FAD reveal a common dominant ultrafast relaxation and a minor slower component. The Lf- transient lacks
H M Said et al.
The American journal of physiology, 266(1 Pt 1), G15-G21 (1994-01-01)
The cellular and molecular regulation of intestinal absorption of the water-soluble vitamin riboflavine (RF) is poorly understood. The availability of a suitable in vitro cultured system that possesses the transport characteristics of the native intestinal absorptive cells would provide a
Yoong-Kee Choe et al.
Journal of computational chemistry, 28(4), 727-739 (2007-01-18)
Time-dependent density functional theory has been applied to investigate the electronic absorption spectrum of oxidized and reduced lumiflavin and its derivative, 8-NH(2)-lumiflavin. The calculations allow the authors to explain the origin of the difference in spectral features between oxidized and
Yasuyuki Yamada et al.
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 11(8), 1007-1023 (2006-09-01)
DNA photolyases (EC 4.1.99.3) are enzymes that catalyze photoreversion of cis,syn-thymine photodimer (T[c,s]T), which is one of major photolesion products in DNA, by utilizing UV light. In this work, we have designed and synthesized Zn2+ -1,4,7,10-tetraazacyclododecane complexes bearing a lumiflavin
Atsuko Satoh et al.
Journal of biochemistry, 134(2), 297-304 (2003-09-11)
The flavoenzyme medium-chain acyl-CoA dehydrogenase (MCAD) eliminates the alpha-proton of the substrate analog, 3-thiaoctanoyl-CoA (3S-C8-CoA), to form a charge-transfer complex with deprotonated 3S-C8-CoA. This complex can simulate the metastable reaction intermediate immediately after the alpha-proton elimination of a substrate and
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