14517-43-2 Usage
Uses
Used in Pharmaceutical Industry:
H-MET-SER-OH is used as a pharmaceutical ingredient for its role in the synthesis of proteins and enzymes, which are essential for various biological functions and therapeutic applications.
Used in Nutritional Supplements:
H-MET-SER-OH is used as a dietary supplement to support protein synthesis and overall health, particularly for individuals with specific dietary needs or those looking to enhance their protein intake.
Used in Cosmetics Industry:
H-MET-SER-OH is used as an active ingredient in cosmetic products for its potential role in skin health and regeneration, leveraging its involvement in protein synthesis and immune system support.
Used in Research and Development:
H-MET-SER-OH is utilized in scientific research as a model compound to study peptide synthesis, protein folding, and enzymatic reactions, contributing to the advancement of biological and medical sciences.
Check Digit Verification of cas no
The CAS Registry Mumber 14517-43-2 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 1,4,5,1 and 7 respectively; the second part has 2 digits, 4 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 14517-43:
(7*1)+(6*4)+(5*5)+(4*1)+(3*7)+(2*4)+(1*3)=92
92 % 10 = 2
So 14517-43-2 is a valid CAS Registry Number.
14517-43-2Relevant academic research and scientific papers
Malinka, M. K.,Stepanov, V. M.,Lobareva, L. S.
, p. 341 - 349 (1982)
A scheme of isolating a highly purified L-amino acylase from Aspergillus oryzae is described which excludes extraction of the enzyme from the preparation "Amilorizin", fractionation with ethanol, chromatography on DEAE-cellulose, and gel filtration through Sephadex G-200 and Bio-Gel P-300.The enzyme, as purified 1240-fold, has a molecular weight of 118,000, apparently consists of two subunits with a molecular weight of 60,000, is stable in the pH range of 7-10 and has an optimum pH of 8.9 and pI of 4.0.Its amino acid composition has been determined and its substrate specificity has been studied.The acylase is a metalloenzyme: Co2+ ions in concentrations of 10-4-5.10-5 M increase the rate of hydrolysis of N-acetyl-L-amino acids three- to fourfold.It shows differences in its molecular and functional properties from acylase I obtained from porcine kidney.
