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20073-81-8

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20073-81-8 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 20073-81-8 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 2,0,0,7 and 3 respectively; the second part has 2 digits, 8 and 1 respectively.
Calculate Digit Verification of CAS Registry Number 20073-81:
(7*2)+(6*0)+(5*0)+(4*7)+(3*3)+(2*8)+(1*1)=68
68 % 10 = 8
So 20073-81-8 is a valid CAS Registry Number.

20073-81-8SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 18, 2017

Revision Date: Aug 18, 2017

1.Identification

1.1 GHS Product identifier

Product name 1-N,3-N-dihydroxybenzene-1,3-dicarboxamide

1.2 Other means of identification

Product number -
Other names 1,3-benzodihydroxamix acid

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:20073-81-8 SDS

20073-81-8Relevant articles and documents

A three dimensional porous metal-organic framework [Fe4L 6·(DMF)3·(H2O)10] constructed from neutral discrete Fe4L6 pyramids [H 2L = 1,3-benzodihydroxamix acid]

Bai, Yan,Guo, Dong,Duan, Chun-Ying,Dang, Dong-Bin,Pang, Ke-Liang,Meng, Qing-Jin

, p. 186 - 187 (2004)

A 3-D porous zeolite-like metal-organic framework surviving guest removal is assembled from a well-defined tetrahedral Fe4L6 cavity by the cooperativity of hydrogen bonds and π-π stacking.

Preparation method of a plurality of (hetero) aromatic polyamines

-

Paragraph 0021-0023, (2021/09/15)

The invention relates to the field of organic functional new material chemicals, and discloses a novel process technology for preparing a plurality of (hetero) aromatic polyamines through corresponding (hetero) aromatic polyfunctional hydroxamic acids (hydroxamic acid) before (re-arrangement). These (hetero) aromatic polyamines are well-known dyes and pigment and pharmaceutical pesticide-related fields of very wide range of critical fine chemical materials.

NADP-dependent glutamate dehydrogenases in a dimorphic zygomycete Benjaminiella poitrasii: Purification, characterization and their evaluation as an antifungal drug target

Deshpande, Mukund V.,Kulkarni, Anand M.,Pathan, Ejaj K.,Prasanna, Nallaballe V. L.,Ramana, Chepuri V.

, (2020/08/21)

Background: It has been reported that the genes coding for NADP-dependent glutamate dehydrogenases (NADP-GDHs) showed a cause-effect relationship with Yeast-Hypha (Y[sbnd]H) reversible transition in a zygomycete Benjaminiella poitrasii. As Y[sbnd]H transition is significant in human pathogenic fungi for their survival and proliferation in the host, the NADP-GDHs can be explored as antifungal drug targets. Methods: The yeast-form specific BpNADPGDH I and hyphal-form specific BpNADPGDH II of B. poitrasii were purified by heterologous expression in E. coli BL-21 cells and characterized. The structural analogs of L-glutamate, dimethyl esters of isophthalic acid (DMIP) and its derivatives were designed, synthesized and screened for inhibition of NADP-GDH activity as well as Y[sbnd]H transition in B. poitrasii, and also in human pathogenic Candida albicans strains. Results: The BpNADPGDH I and BpNADPGDH II were found to be homo-hexameric proteins with native molecular mass of 282 kDa and 298 kDa, respectively and subunit molecular weights of 47 kDa and 49 kDa, respectively. Besides the distinct kinetic properties, BpNADPGDH I and BpNADPGDH II were found to be regulated by cAMP-dependent- and Calmodulin (CaM) dependent- protein kinases, respectively. The DMIP compounds showed a more pronounced effect on H-form specific BpNADPGDH II and inhibited Y[sbnd]H transition as well as growth in B. poitrasii and C. albicans strains. Conclusion: The present study will be useful to design and develop antifungal drugs against dimorphic human pathogens using glutamate dehydrogenase as a target. Significance: Glutamate dehydrogenases can be explored as a target against human pathogenic fungi.

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