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68423-35-8

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68423-35-8 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 68423-35-8 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 6,8,4,2 and 3 respectively; the second part has 2 digits, 3 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 68423-35:
(7*6)+(6*8)+(5*4)+(4*2)+(3*3)+(2*3)+(1*5)=138
138 % 10 = 8
So 68423-35-8 is a valid CAS Registry Number.

68423-35-8Relevant articles and documents

SUPRAMOLECULAR PROTEIN ASSEMBLIES WITH ADVANCED FUNCTIONS AND SYNTHESIS THEREOF

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Paragraph 0367-0368, (2019/05/18)

The present invention discloses stimuli-sensitive protein conjugate which can make supramolecular protein assemblies and methods for using the same. The present invention provides simple and rational process for construction of said stimuli-sensitive spherical protein assemblies through supramolecular chemical strategy.

Crystal structure of the Homo sapiens kynureninase-3-hydroxyhippuric acid inhibitor complex: Insights into the molecular basis of kynureninase substrate specificity

Lima, Santiago,Kumar, Sunil,Gawandi, Vijay,Momany, Cory,Phillips, Robert S.

experimental part, p. 389 - 396 (2009/10/01)

Homo sapiens kynureninase is a pyridoxal-5'-phosphate dependent enzyme that catalyzes the hydrolytic cleavage of 3-hydroxykynurenine to yield 3-hydroxyanthranilate and L-alanine as part of the tryptophan catabolic pathway leading to the de novo biosynthesis of NAD+. This pathway results in quinolinate, an excitotoxin that is an NMDA receptor agonist. High levels of quinolinate have been correlated with the etiology of neurodegenerative disorders such as AIDS-related dementia and Alzheimer's disease. We have synthesized a novel kynureninase inhibitor, 3-hydroxyhippurate, cocrystallized it with human kynureninase, and solved the atomic structure. On the basis of an analysis of the complex, we designed a series of His- 102, Ser-332, and Asn-333 mutants. The H102W/N333T and H102W/S332G/N333T mutants showed complete reversal of substrate specificity between 3-hydroxykynurenine and L-kynurenine, thus defining the primary residues contributing to substrate specificity in kynureninases.

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