Experimental Study on Hydroxylation of Hydroxylamine /Guanidine Hydrochloride(cas 50-01-1) to Pyricot
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    Microcalorimetric Study on Denaturation of Bovine Hemoglobin Induced by Guanidine Hydrochloride(cas 50-01-1)
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    Study on denaturation of lysozyme in guanidine hydrochloride(50-01-1) solution by fluorescence phase diagram method
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    THz Time - Domain Spectra Study on Chlorophyll Induced by Guanidine Hydrochloride(50-01-1)
    Study on Equilibrium Dialysis of Urea and Guanidine Hydrochloride(50-01-1) on Lysozyme Molecules
    Effect on the spectral characteristics of guanidine hydrochloride(50-01-1) Bi Salicornia thylakoid membrane protein
   
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Guanidine hydrochloride


Chemical Name:Guanidine hydrochloride
CAS No.:50-01-1
Appearance: White crystal powder
Molecular Formula:CH5N3·HCl
Molecular Weight:95.53
Packing: 25kg plastic woven bag
Application: 50-01-1 is mainly used in pharmaceuticals,  pesticide, dye, other organicsynthesis  intermediates, antistatic agent of
synthetic fibre and other fields.It's a very important raw material for manufacture of sulfa drugs and folic. 

Guanidine hydrochloride(50-01-1) description:
Guanidine hydrochloride(50-01-1) is a strong organic base existing primarily as guanidium ions at physiological pH. It is found in the urine as a normal product of protein metabolism. It is also used in laboratory research as a protein denaturant.It is also used in the treatment of myasthenia and as a fluorescent probe in HPLC.
Guanidine hydrochloride(50-01-1) is the hydrochloride salt form of guanidine, a strong basic compound with parasympathomimetic activity. Guanidine hydrochloride(50-01-1) enhances the release of acetylcholine following a nerve impulse and potentiates acetylcholine actions on muscarinic and nicotinic receptors. It also appears to slow the rates of depolarization and repolarization of muscle cell membranes.
Guanidine hydrochloride(50-01-1) is a powerful, chaotropic agent which is widely used for purification of proteins and nucleic acids. Guanidine hydrochloride(50-01-1) is useful for denaturation and refolding of proteins as well as in the recovery of periplasmic proteins and isolation of RNA. At higher concentrations, this strong denaturant has been reported to solubilize denatured insoluble proteins such as inclusion bodies. When utilized at lower concentrations, Guanidine Hydrochloride is noted to be useful in prompting the refolding of denatured proteins. Guanidine hydrochloride(50-01-1) is also been reported to allow return of enzymatic activity in protocols using Guanidine hydrochloride(50-01-1) as a first step. Guanidine hydrochloride(50-01-1) is an inhibitor of RNase.
Guanidine hydrochloride(50-01-1) is used for purification of proteins and nucleic acids. It can be used as a medicine, organic synthesis intermediate and is used in dyes. It acts as an intermediate in the preparation of sulfadiazine, which is an important raw material for sulfamethyldiazine, sulfamethazine and folic acid. It is utilized in the synthesis of 2-amino-pyrimidine, 2-amino-6-methyl-pyrimidine and 2-amino-4,6-dimethyl-pyrimidine. Also used in RNA isolation to dissociate nucleoproteins and inhibit RNase.
Guanidine hydrochloride(50-01-1) or guanidine hydrochloride, usually abbreviated GuHCl and sometimes GdnHCl or GdmCl, is the hydrochloride salt of guanidine.

Guanidine hydrochloride(50-01-1) structure:
Guanidine hydrochloride(50-01-1) crystallizes in orthorhombic space group Pbca. The crystal structure consists of a network of guanidinium cations and chloride anions linked by N–H···Cl hydrogen bonds.

Guanidine hydrochloride(50-01-1) use in protein denaturation:
Guanidine hydrochloride(50-01-1) (GdnHCl) is a better denaturant than urea.It should normally give higher and lower values for m and for Cm, respectively, but identical deltaG° values. Since m values in both denaturants can be predicted/estimated from the size of the protein (Myers et al., 1995) and delatG° should not change, yes it is possible - in principle - to predict Cm in one denaturant, knowing its value in the other.
but to have a general correlation co-efficient is almost impossible as every protein has unique folding. Though such co-relation may be found for a special protein fold, but what purpose it may serve apart from giving a tentative idea that GdnHCl or urea may be a better denaturant! If you are looking for even better denaturant than Gdn HCl then use GdnSCN, it is better and more effective.
Guanidinium chloride is a strong chaotrope and one of the strongest denaturants used in physiochemical studies of protein folding. At high concentrations of guanidinium chloride (e.g., 6 M), proteins lose their ordered structure, and they tend to become randomly coiled, i.e. they do not contain any residual structure. However, at concentrations in the millimolar range in vivo, guanidinium chloride has been shown to "cure" prion positive cells (i.e. cells exhibiting a prion positive phenotype revert to a prion negative phenotype). This is the result of inhibition of the Hsp104 chaperone protein known to play an important role in prion fiber fragmentation and propagation.

Guanidine hydrochloride(50-01-1) historical survey:
Petrunkin and Petrunkin (1927, 1928) appear to be the first who studied the binding of GndCl to gelatin and a mixture of thermally denatured protein from brain extract. Greenstein (1938, 1939), however, appears to be the first to discover the high denaturing action of guanidinium halides and thiocyanates in following the liberation of sulfhydryl groups in ovalbumin and few other proteins as a function of salt concentration.

Guanidine hydrochloride(50-01-1) medical Uses:
Guanidine hydrochloride(50-01-1) is indicated for the reduction of the symptoms of muscle weakness and easy fatigability associated with Eaton-Lambert syndrome. It is not indicated for treating myasthenia gravis. It apparently acts by enhancing the release of acetylcholine following a nerve impulse. It also appears to slow the rates of depolarization and repolarization of muscle cell membranes. Initial dosage is usually between 10 and 15 mg/kg (5 to 7 mg/pound) of body weight per day in 3 or 4 divided doses. This dosage may be gradually increased to a total daily dosage of 35 mg/kg (16 mg/pound) of body weight per day or up to the development of side effects. Side effects include increased peristalsis and diarrhea. Fatal bone-marrow suppression, apparently dose related, can occur with guanidine.
Drug intermediates:
Guanidine hydrochloride(50-01-1) drug used primarily as an intermediate in the manufacture of sulfadiazine, an important raw material sulfamethyldiazine, sulfamethazine and folic acid.
Guanidine hydrochloride(50-01-1) (or guanidine nitrate) and ethyl cyanoacetate reaction, cyclization of 2,4-diamino-6-hydroxy pyrimidine, folic acid for the synthesis of antianemic. Furthermore guanidine hydrochloride also used synthetic anti-static agent.
A cyclic guanidine hydrochloride(50-01-1) capsules:
[Properties]capsules, yellow powder inside it.
[Toxicology] This product is a broad-spectrum antimicrobial agent which has a bactericidal effect when applied at high concentrations. The product has certain antibacterial effects on Streptococcus pneumoniae, hemolytic streptococcus, staphylococcus and some grass lotus bacteria, Clostridium perfringens, Bacillus anthracis, Yersinia pestis, diphtheria, tetanus, Brucella spp, Haemophilus influenzae, bending spp., and Vibrio cholerae. It also has inhibitory effects on Rickettsia, mycoplasma, Chlamydia, spirochetes, and some protozoa. However, Enterobacteriaceae such as Escherichia coli, Klebsiella, Salmonella, and Shigella are mostly resistant to this product. This product has a better effect on Gram-positive bacteria than gram-negative bacteria, but Enterococcus is resistant to it. Others species such as Actinomyces, Bacillus anthracis, Listeria monocytogenes bacteria, Clostridium spp and Nocardia, are also sensitive to the chemical. Neisseria gonorrhoeae which is resistant to this product is also resistant to tetracycline. The product has a certain antibacterial effect on Neisseria gonorrhoeae and Neisseria meningitidis with a certain antibacterial activity, but penicillin-resistant Neisseria gonorrhoeae is also resistant to tetracycline. This mechanism of action of this product is that it can specifically bind to the A site of bacterial 30S ribosomal subunit, blocking the attach of aminoacyl-tRNA into this site, and thus blocking the growth of the peptide chain and the overall protein synthesis.
[Pharmacokinetics] This product has a high solubility in water, and can be rapidly absorbed after oral administration. The blood concentration reaches highest within 3 hours with effective blood concentration being maintained for 12 hours. Compared with other tetracyclines, its main feature is its great affinity to bronchial and lung tissue. It has a much higher concentration in the bronchus, lung tissue and bronchial secretions than comparable amount tetracycline hydrochloride after orally administration. Its concentration in the blood can be maintained at a higher level and longer period than tetracycline. It is mainly excreted by urine in its active form.
[Indications]For respiratory infections caused by sensitive strains.
[Dosage] Oral administration. Day 1.2g (12 grains), three to four times daily.
[Specification] 0.1g (10 million units).
[Storage] sealed and kept in a dry, cool and dark place.

Purification of inclusion body proteins:
Denaturing agents (urea and guanidine hydrochloride(50-01-1)) can break the hydrogen bond in the protein structure, which increases the solubility of non-polar molecules including the side chains of amino acid, reducing the hydrophobic interaction; Urea can also deep into the interior of the protein molecule to affect the close packing state of protein molecules. In addition, detergents, organic solvents, heavy metals, heat, mechanical forces, freezing, ultrasound, high pressure, radiation, etc. all can cause protein denaturation. These kinds of denaturation are only related to disrupting the secondary bond interaction such as the hydrogen bond, salt bond, hydrophobic interactions, van der Waals interactions without breaking the covalent bonds. Some denatured proteins can automatically restore into its natural conformation after the denaturation factors have been removed, a phenomenon known as protein refolding (re-naturation), namely that re-folding in the field of protein folding research.
Inclusion body protein purification:
Most conditions are at pH8, usually use strong denaturing agents such as urea (6-8mol/L), guanidine hydrochloride (Gdn-HCl 5~8 mol/L or 6mol/L), to disrupt any kinds of chemical bonds within or between protein molecules through the interactions between ions, and thus stretching the polypeptide. In general, Gdn-HCl is better than urea due to that Gdn-HCl is stronger denaturant than urea, which enables the dissolution of inclusion bodies which cannot be dissolved by urea. Moreover, urea has an issue that it decomposed isocyanate can cause the formylation of the free amino groups of the polypeptide, especially for long-term incubation at alkaline pH condition. Using detergents such as SDS, n-hexadecyl-trimethyl ammonium chloride, or Sarkosyl, etc., which can disrupt the hydrophobic bonding within the protein, can also dissolve the inclusion body proteins. Moreover, we can use TritonX-100 to dissolve the protein inclusion bodies of Zymononas mobilis levansucrase. In addition, for the cysteine-containing proteins, their isolated inclusion bodies generally contain a number of inter-chain disulfide bonds and non-active disulfide bonds within chain. For these inclusion bodies, we can apply some organic solution, alkaline environment (greater than 9) or acid (70% formic acid) to dissolve them.
We need to add a reducing agent in denaturing solution such as 2-mercaptoethanol (β-ME), dithiothreitol (of DTT), dithioerythritol alcohols, reduced glutathione (GST), and the cysteine. Concentration of the reducing agent is generally 50-100mM β-ME or DTT. Some literature also use 5mM. The concentration of the reducing agent has nothing to do with the number of the disulfide bonds. For proteins without disulfide bonds, adding or not reducing reagent doesn’t make any difference, such as improving the dissolution of inclusion bodies of bovine growth hormone. For the inclusion bodies of certain target proteins without disulfide bonds, sometimes it is still necessary to use a reducing agent which may be due to that disulfide bonds-containing impure protein affects the dissolution of inclusion bodies. Also we need to add a metal chelating agent such as EDTA or EGTA, to chelate metal ions such as Cu2+, Fe2+ prevent the oxidation reaction between the reduced thiol groups with them. After the dissolution of denaturant, protein will lose its biological activity.

Guanidine hydrochloride(50-01-1) uses: 
Guanidine hydrochloride(50-01-1) is used in RNA isolation to dissociate nucleoproteins and inhibit RNase.
Strong chaotropic agent useful for the denaturation and subsequent refolding of proteins. This strong denaturant can solubilize insoluble or denatured proteins such as inclusion bodies. This can be used as the first step in refolding proteins or enzymes into their active form. Urea and dithiothreitol (DTT) may also be necessary.

1. For organic synthesis and pharmaceutical industry.
2. Mainly used as a pharmaceutical intermediate; an important raw material for producing sulfadiazine, sulfamethyldiazine, sulfamethazine and folic acid.
3. Used as intermediates for synthesis of medicine, pesticides, dyes and other organics. For synthesis of 2-amino-pyrimidine, 2-amino-6-methyl-pyrimidine, and 2-amino-4,6-dimethyl-pyrimidine. A intermediate for producing sulfadiazine, sulfamethyldiazine, and sulfamethazine. Guanidine hydrochloride(50-01-1) (or guanidine nitrate) can be reacted with ethyl cyanide for cyclization into 2,4-diamino-6-hydroxy-pyrimidine. This is for synthesis of anti-anemia drugs: folic acid. It can also be used for the synthesis of anti-static agent of synthetic fiber.

50-01-1

 
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