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3422-39-7

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3422-39-7 Usage

Uses

H-Glu-Tyr-OH is an Angiotensin-?converting enzyme (ACE) inhibitory peptide derived from food proteins widely reported for hypertension treatment.

Check Digit Verification of cas no

The CAS Registry Mumber 3422-39-7 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 3,4,2 and 2 respectively; the second part has 2 digits, 3 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 3422-39:
(6*3)+(5*4)+(4*2)+(3*2)+(2*3)+(1*9)=67
67 % 10 = 7
So 3422-39-7 is a valid CAS Registry Number.
InChI:InChI=1/C14H18N2O6/c15-10(5-6-12(18)19)13(20)16-11(14(21)22)7-8-1-3-9(17)4-2-8/h1-4,10-11,17H,5-7,15H2,(H,16,20)(H,18,19)(H,21,22)/t10-,11+/m0/s1

3422-39-7SDS

SAFETY DATA SHEETS

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

Version: 1.0

Creation Date: Aug 16, 2017

Revision Date: Aug 16, 2017

1.Identification

1.1 GHS Product identifier

Product name 4-amino-5-[[1-carboxy-2-(4-hydroxyphenyl)ethyl]amino]-5-oxopentanoic acid

1.2 Other means of identification

Product number -
Other names H-Glu-Tyr-OH

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:3422-39-7 SDS

3422-39-7Downstream Products

3422-39-7Relevant articles and documents

A new tyrosine-specific chymotrypsin-like and angiotensin-degrading serine proteinase from Vipera lebetina snake venom

Siigur, Ene,T?nism?gi, Külli,Trummal, Katrin,Samel, Mari,Vija, Heiki,Aasp?llu, Anu,R?nnholm, Gunilla,Subbi, Juhan,Kalkkinen, Nisse,Siigur, Jüri

experimental part, p. 321 - 330 (2012/01/06)

Vipera lebetina venom contains different metallo- and serine proteinases that affect coagulation and fibrin(ogen)olysis. A novel serine proteinase from V. Lebetina venom having ChymoTrypsin Like Proteolytic activity (VLCTLP) was purified to homogeneity from the venom using Sephadex G-100sf, DEAE-cellulose, heparin-agarose and FPLC on Superdex 75 chromatographies. VLCTLP is a glycosylated serine proteinase with a molecular mass of 41926 Da. It reacts with N-acetyl-l-tyrosine ethyl ester (ATEE) but not with Suc-Ala-Ala-Pro-Phe-pNA or Suc-Ala-Ala-Pro-Leu-pNA. The complete amino acid sequence of the VLCTLP is deduced from the nucleotide sequence of the cDNA encoding this protein. The full-length cDNA sequence of the VLCTLP encodes open reading frame of 257 amino acid residues that includes a putative signal peptide of 18 amino acids, a proposed activation peptide of six amino acid residues and serine proteinase of 233 amino acid residues. VLCTLP belongs to the S1 (chymotrypsin) subfamily of proteases. The multiple alignment of its deduced amino acid sequence showed structural similarity with other serine proteases from snake venoms. The protease weakly hydrolyses azocasein, Aα-chain and more slowly Bβ-chain of fibrinogen. VLCTLP does not cleave fibrin and has no gelatinolytic activity. Specificity studies against peptide substrates (angiotensin I and II, oxidized insulin B-chain, glucagon, fibrinogen fragments etc.) showed that VLCTLP catalysed the cleavage of peptide bonds after tyrosine residues. VLCTLP is the only purified and characterized serine proteinase from snake venoms that catalyses ATEE hydrolysis. We detected ATEE-hydrolysing activities also in 9 different Viperidae and Crotalidae venoms.

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