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307394

Sigma-Aldrich

Guanidine sulfate salt

99%

Sinônimo(s):

Bisguanidinium sulfate, Guanidinium sulfate

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About This Item

Fórmula linear:
[NH2C(=NH)NH2]2 · H2SO4
Número CAS:
Peso molecular:
108.11
Beilstein:
3632154
Número CE:
Número MDL:
Código UNSPSC:
12352100
ID de substância PubChem:
NACRES:
NA.22

Ensaio

99%

forma

powder

pf

290-293 °C (dec.) (lit.)

cadeia de caracteres SMILES

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)

chave InChI

UYAKTBUPMOOXNW-UHFFFAOYSA-N

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Descrição geral

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

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Equipamento de proteção individual

Eyeshields, Gloves, type N95 (US)


Certificados de análise (COA)

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Guanidina

SAFC

PHG0006

Guanidina

Guanidina ≥99% (titration), organic base and chaeotropic agent

Sigma-Aldrich

G4505

Guanidina

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)
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
Vera G Grivennikova et al.
Biochimica et biophysica acta, 1827(3), 446-454 (2013-01-15)
Membrane-bound respiratory complex I in inside-out submitochondrial particles (SMP) catalyzes both superoxide and hydrogen peroxide formation in NADH- and/or succinate-supported reactions. At optimal NADH concentration (50μM), the complex I-mediated process results in a formation of two superoxide anions and H(2)O(2)

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