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Phenylthiohydantoin glutamic acid (PTH-Glu) is a chemical compound derived from the reaction of glutamic acid with phenylisothiocyanate, a process known as Edman degradation. This reaction is used in protein sequencing to identify the N-terminal amino acid of a peptide or protein. PTH-Glu is formed when glutamic acid, an amino acid with a carboxyl group and a side chain containing a carboxyl group, reacts with phenylisothiocyanate, resulting in a phenylthiocarbamoyl derivative. PHENYLTHIOHYDANTOIN GLUTAMIC ACID) is then cleaved from the peptide chain, and its identity can be determined through chromatographic techniques, providing crucial information about the protein's sequence. PTH-Glu is a key intermediate in this process, allowing scientists to deduce the order of amino acids in a protein, which is essential for understanding its structure and function.

7390-22-9

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7390-22-9 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 7390-22-9 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 7,3,9 and 0 respectively; the second part has 2 digits, 2 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 7390-22:
(6*7)+(5*3)+(4*9)+(3*0)+(2*2)+(1*2)=99
99 % 10 = 9
So 7390-22-9 is a valid CAS Registry Number.
InChI:InChI=1/C12H12N2O3S/c15-10(16)7-6-9-11(17)14(12(18)13-9)8-4-2-1-3-5-8/h1-5,9H,6-7H2,(H,13,18)(H,15,16)/t9-/m0/s1

7390-22-9Relevant academic research and scientific papers

Simple and Efficient Synthesis of 5-Substituted-3-phenyl-2-thioxoimidazolidin-4-one Derivatives from S -Amino Acids and Phenylisothiocyanate in et 3N/DMF-H 2O

Jangale, Asha D.,Wagh, Yogesh B.,Tayade, Yogesh A.,Dalal, Dipak S.

supporting information, p. 1876 - 1886 (2015/08/03)

A concise approach for the transformation of various S-amino acids into the 5-alkyl-3-phenyl-2-thioxoimidazolidin-4-one heterocycles using phenylisothiocyanate is described. Phenylthiohydantoins of amino acid were synthesized at room temperature in Et3N/DMF-H2O with easy workup and excellent yields.

Modulation of the pharmacological activities of secretory phospholipase A2 from Crotalus durissus cascavella induced by naringin

Santos, Marcelo L.,Toyama, Daniela O.,Oliveira, Simone C. B.,Cotrim, Camila A.,Diz-Filho, Eduardo B. S.,Fagundes, Fabio H. R.,Soares, Veronica C. G.,Aparicio, Ricardo,Toyama, Marcos H.

experimental part, p. 738 - 761 (2011/04/15)

In this work we have characterized the action of the naringin, a flavonoid found in grapefruit and known for its various pharmacological effects, which include antioxidant, blood lipid lowering and anticancer activity, on the structure and biochemical activities of a secretory phospholipase A (sPLA2) from Crotalus durissus cascavella, an important protein involved in the releasinge of arachidonic acid in phospholipid membranes. sPLA2 was incubated with naringin (mol:mol) at 37 °C and a discrete reduction in the UV scanning signal and a modification of the circular dichroism spectra were observed after treatment with naringin, suggesting modifications of the secondary structure of the protein. This flavonoid was able to decrease enzymatic activity and some pharmacological effects, such as myonecrosis, platelet aggregation, and neurotoxic activity caused by sPLA2, however, the inflammatory effect was not affected by naringin. In addition, small angle X-ray scattering (SAXS) data were collected for sPLA2 and naringin-treated sPLA2 to evaluate possible modifications of the protein structure. These structural investigations have shown that sPLA2 is an elongated dimer in solution and after treatment with naringin a conformational change in the dimeric configuration was observed. Our results suggest that structural modification may be correlated with the loss of enzymatic activity and alterations in pharmacological properties.

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