7763-16-8 Usage
Uses
Used in Enzymology Research:
Z-GLN-ONP is used as a substrate in enzymology research for the purpose of measuring the activity of enzymes that can cleave peptide bonds. The release of a yellow-colored product upon enzymatic cleavage allows for easy detection and quantification of enzyme activity.
Used in Biochemistry Studies:
In biochemistry, Z-GLN-ONP is employed as a tool to study the mechanisms and characteristics of enzymes involved in peptide bond cleavage. Z-GLN-ONP's ability to produce a detectable product upon cleavage provides a convenient method for analyzing enzyme function and interactions.
Used in Diagnostic Applications:
Z-GLN-ONP can be utilized in diagnostic applications to assess the activity of specific enzymes, which may be indicative of certain diseases or conditions. Z-GLN-ONP's reactivity and the ease of detecting the yellow-colored product make it a valuable tool for clinical and laboratory settings.
Used in Pharmaceutical Development:
Z-GLN-ONP may also be used in the development of pharmaceuticals, particularly in the design and testing of enzyme inhibitors or activators. Z-GLN-ONP's ability to measure enzyme activity can aid in the identification of potential drug candidates and their effectiveness in modulating enzyme function.
Check Digit Verification of cas no
The CAS Registry Mumber 7763-16-8 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 7,7,6 and 3 respectively; the second part has 2 digits, 1 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 7763-16:
(6*7)+(5*7)+(4*6)+(3*3)+(2*1)+(1*6)=118
118 % 10 = 8
So 7763-16-8 is a valid CAS Registry Number.
InChI:InChI=1/C19H19N3O7/c20-17(23)11-10-16(21-19(25)28-12-13-4-2-1-3-5-13)18(24)29-15-8-6-14(7-9-15)22(26)27/h1-9,16H,10-12H2,(H2,20,23)(H,21,25)
7763-16-8Relevant articles and documents
Peptide coupling of unprotected amino acids through in situ p-nitrophenyl ester formation
Gagnon, Paul,Huang, Xicai,Therrien, Eric,Keillor, Jeffrey W.
, p. 7717 - 7719 (2007/10/03)
Several series of dipeptides and tripeptides were prepared via an activation-coupling method involving the in situ formation of a p-nitrophenyl ester of an (N-protected) amino acid, followed by coupling with an unprotected amino acid in partially aqueous solutions. The resulting peptide is easily isolated by precipitation. In general, the yields obtained are good to excellent and racemization is minimal. This method is particularly advantageous with respect to its simplicity and lack of obligatory side chain protection/deprotection steps.
Dichlorotris(dimethylamino)phosphorane as Dehydration Reagent for the Preparation of Activated (-ONp, -OPcp, -NSu)Esters of N-Protected Multifunctional Amino Acids
Appel, Rolf,Glaesel, Ursula
, p. 3511 - 3516 (2007/10/02)
Dichlorotris(dimethylamino)phosphorane (5) is an excellent reagent for the preparation of the activated esters of N-protected amino acids 7-9.Besides 4-nitrophenyl-, pentachlorophenyl-, and N-hydroxysuccinimide esters of various N-protected amino acids, in the presence of HOBt benzyloxycarbonyl-threonine N-hydroxysuccinimide ester was obtained for the first time.
