Merck
CN
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文件

安全信息

307394

Sigma-Aldrich

胍 硫酸盐

99%

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别名:
Bisguanidinium sulfate, Guanidinium sulfate
线性分子式:
[NH2C(=NH)NH2]2 · H2SO4
CAS号:
594-14-9
分子量:
108.11
Beilstein:
3632154
EC 号:
209-826-8
MDL编号:
MFCD00013115
PubChem化学物质编号:
24858588
NACRES:
NA.22

质量水平

100

检测方案

99%

形式

powder

mp

290-293 °C (dec.) (lit.)

SMILES字符串

NC(N)=N.NC(N)=N.OS(O)(=O)=O

InChI

1S/2CH5N3.H2O4S/c2*2-1(3)4;1-5(2,3)4/h2*(H5,2,3,4);(H2,1,2,3,4)

InChI key

UYAKTBUPMOOXNW-UHFFFAOYSA-N

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相关类别

一般描述

The multicomponent condensation of guanidine sulfate salt with H2S and CH2O was studied.

储存分类代码

11 - Combustible Solids

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

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Multicomponent reactions of urea and its derivatives with CH2O and H2S in the synthesis of 1, 3, 5-thiadiazinane-4-(thi) ones and macroheterocycles.
ARKIVOC (Gainesville, FL, United States), 8, 149-162 (2011)
Christoph J O Kaiser et al.
Nature communications, 4, 1571-1571 (2013-03-14)
Neurodegeneration is linked to protein aggregation in several human disorders. In Huntington's disease, the length of a polyglutamine stretch in Huntingtin is correlated to neuronal death. Here we utilize a model based on glutamine stretches of 0, 30 or 56
Yuling Shao et al.
Journal of molecular graphics & modelling, 40, 54-63 (2013-01-29)
Density functional theory and volume-based thermodynamics calculations have been performed to study the crystal densities, heats of formation (HOFs), energetic properties, and thermodynamics of formation for a series of ionic salts composed of triaminoguanidinium or ammonium cations and tetrazole-based anions.
Michal R Szymanski et al.
Biochemistry, 52(11), 1858-1873 (2013-02-20)
Thermodynamic and structural characteristics of the Escherichia coli DnaT protein trimerization reaction have been quantitatively examined using fluorescence anisotropy and analytical ultracentrifugation methods. Binding of magnesium to the DnaT monomers regulates the intrinsic affinity of the DnaT trimerization reaction. Comparison
Eva Kummer et al.
FEBS letters, 587(6), 810-817 (2013-02-19)
The Saccharomyces cerevisiae AAA+ protein Hsp104 and its Escherichia coli counterpart ClpB cooperate with Hsp70 chaperones to refold aggregated proteins and fragment prion fibrils. Hsp104/ClpB activity is regulated by interaction of the M-domain with the first ATPase domain (AAA-1), controlling
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