87831-94-5 Usage
Description
H-LEU-ALA-NH2 HCL is a chemical compound consisting of the amino acids leucine and alanine linked together to form a peptide chain, with the hydrochloride salt form indicated by "HCL" in its name. It is widely utilized in biochemical and pharmaceutical research for the synthesis of peptides and complex molecules, as well as in the study of protein structure and function.
Uses
Used in Biochemical and Pharmaceutical Research:
H-LEU-ALA-NH2 HCL is used as a building block for the synthesis of peptides and other complex molecules, contributing to the development of new drugs and pharmaceutical products.
Used in Protein Structure and Function Studies:
H-LEU-ALA-NH2 HCL is employed in the study of protein structure and function, aiding in the understanding of their roles in biological processes and potential therapeutic applications.
Used in Drug Development:
H-LEU-ALA-NH2 HCL may have potential applications in the treatment of various diseases and medical conditions. It can be modified and engineered to exhibit specific biological activities, making it a valuable component in the development of innovative pharmaceuticals.
Check Digit Verification of cas no
The CAS Registry Mumber 87831-94-5 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 8,7,8,3 and 1 respectively; the second part has 2 digits, 9 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 87831-94:
(7*8)+(6*7)+(5*8)+(4*3)+(3*1)+(2*9)+(1*4)=175
175 % 10 = 5
So 87831-94-5 is a valid CAS Registry Number.
87831-94-5Relevant articles and documents
Peptide Synthesis by Means of Immobilized Enzymes II. Immobilized Trypsin, Thermolysin and Papain
Koennecke, Andreas,Haensler, Marion,Schellenberger, Volker,Jakubke, Hans-Dieter
, p. 433 - 444 (1983)
Model studies were performed on the utility of covalently immobilized trypsin, thermolysin and papain for peptide bond formation.Trypsin and thermolysin catalyzed the formation of peptide bonds with nearly the same efficiency as the soluble proteases and they could be re-used successfully for further coupling experiments.The possibility of using immobilized trypsin and papain for kinetically controlled peptide bond formation was investigated.With the serine type enzyme trypsin excellent product yields were obtained starting with ester carboxyl components and an economical ratio of substrates.Experiments with the thiol protease papain were unsatisfactory because the once formed product is hydrolyzed as fact as the starting ester substrate used. - Keywords: Immobilized enzymes; Papain; Peptide synthesis; Thermolysin; Trypsin