方案
99.9%
表单
tubes
制造商/商品名称
Goodfellow 567-264-99
电阻率
5.0 μΩ-cm, 20°C
长度 × 壁厚度
200 mm × 0.15 mm
外径 × 内径
1.0 mm × 0.7 mm
沸点
4612 °C (lit.)
mp
2617 °C (lit.)
密度
10.3 g/mL at 25 °C (lit.)
SMILES字符串
[Mo]
InChI
1S/Mo
InChI key
ZOKXTWBITQBERF-UHFFFAOYSA-N
一般描述
For updated SDS information please visit www.goodfellow.com.
法律信息
Product of Goodfellow
法规信息
新产品
此项目有
Manuel Tejada-Jiménez et al.
Metallomics : integrated biometal science, 5(9), 1191-1203 (2013-06-27)
The viability of plants relies on molybdenum, which after binding to the organic moiety of molybdopterin forms the molybdenum cofactor (Moco) and acquires remarkable redox properties. Moco is in the active site of critical molybdoenzymes, which use to work as
Ralf R Mendel
BioFactors (Oxford, England), 35(5), 429-434 (2009-07-23)
The transition element molybdenum (Mo) is an essential micronutrient that is needed as catalytically active metal during enzyme catalysis. In humans four enzymes depend on Mo: sulfite oxidase, xanthine oxidoreductase, aldehyde oxidase, and mitochondrial amidoxime reductase. In addition to these
Tingyu Shi et al.
Journal of cellular biochemistry, 112(10), 2721-2728 (2011-06-17)
When intracelluar pathogens enter the host macrophages where in addition to oxidative and antibiotic mechanisms of antimicrobial activity, nutrients are deprived. Human pathogen Mycobacterium tuberculosis is one of macrophage parasitisms, which can replicate and persist for decades in dormancy state
Angel Llamas et al.
Metallomics : integrated biometal science, 3(6), 578-590 (2011-05-31)
Molybdenum (Mo) is a very scarce element whose function is fundamental in living beings within the active site of Mo-oxidoreductases, playing key roles in the metabolism of N, S, purines, hormone biosynthesis, transformation of drugs and xenobiotics, etc. In eukaryotes
Yilin Hu et al.
Microbiology and molecular biology reviews : MMBR, 75(4), 664-677 (2011-12-01)
Nitrogenase catalyzes a key step in the global nitrogen cycle, the nucleotide-dependent reduction of atmospheric dinitrogen to bioavailable ammonia. There is a substantial amount of interest in elucidating the biosynthetic mechanisms of the FeMoco and the P-cluster of nitrogenase, because
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