38972-84-8 Usage
Uses
Used in Biochemical Research:
2',3',5'-Triacetylinosine is used as a precursor in the synthesis of certain nucleosides for biochemical research. Its acetylated structure allows for the creation of modified nucleosides that can be used to study the interactions and functions of nucleic acids in biological systems.
Used in Pharmaceutical Development:
2',3',5'-Triacetylinosine is used as an experimental compound in nucleic acid research for pharmaceutical development. Its unique properties may contribute to the discovery of new drugs or therapeutic agents that can target specific biological processes or diseases.
Used in Drug Synthesis:
2',3',5'-Triacetylinosine is used as a key intermediate in the synthesis of various pharmaceutical compounds. Its acetylated ribose sugar can be further modified or used as a building block to create new drug molecules with potential therapeutic applications.
Used in Diagnostic Applications:
2',3',5'-Triacetylinosine is used as a component in the development of diagnostic tools, such as molecular probes or imaging agents, that can be used to detect or monitor diseases at the molecular level. Its unique chemical properties may enable the creation of more sensitive or specific diagnostic assays.
Check Digit Verification of cas no
The CAS Registry Mumber 38972-84-8 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 3,8,9,7 and 2 respectively; the second part has 2 digits, 8 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 38972-84:
(7*3)+(6*8)+(5*9)+(4*7)+(3*2)+(2*8)+(1*4)=168
168 % 10 = 8
So 38972-84-8 is a valid CAS Registry Number.
InChI:InChI=1/C16H18N4O5/c21-14(20-13(15(22)23)6-12-7-17-10-19-12)8-18-16(24)25-9-11-4-2-1-3-5-11/h1-5,7,10,13H,6,8-9H2,(H,17,19)(H,18,24)(H,20,21)(H,22,23)
38972-84-8Relevant academic research and scientific papers
Protease-catalysed synthesis of peptides containing histidine and lysine
Beck-Piotraschke, Karin,Jakubke, Hans-Dieter
, p. 1505 - 1518 (2007/10/03)
The kinetically controlled α-chymotrypsin- and trypsin-catalysed syntheses of peptides starting from simple acyl donor esters containing histidine at the P1-position (nomenclature according to Schechter and Berger) and lysine derivatives as amino components were examined on the basis of their kinetic parameters. Despite higher specificity constants (k(cat)/K(M)) of trypsin-catalysed ester hydrolysis, α-chymotrypsin- catalysed acyl transfer to N(ε)unprotected lysine derivatives gave higher peptide yields as compared to trypsin-catalysed reactions, whereas in acyl transfer to N(ε)-protected lysine derivatives the trypsin-catalysed reaction gave higher yields. α-Chymotrypsin-catalysed acyl transfer reactions in frozen systems demonstrated the yield-enhancing effect of freezing. Using specific ester leaving groups, both the amount of enzyme and the reaction time can be reduced. In frozen systems the ε-amino function of H-Lys-OH acts as an acyl acceptor at pH ≤9.
