14517-43-2 Usage
General Description
H-MET-SER-OH is a chemical compound consisting of three amino acids: histidine (H), methionine (MET), and serine (SER) joined together in a peptide chain. It is an important building block for proteins and enzymes in biological systems. Histidine is an essential amino acid that is involved in the formation of hemoglobin and certain enzyme reactions. Methionine plays a crucial role in protein synthesis and the metabolism of lipids. Serine is a non-essential amino acid that is important for the synthesis of proteins and the maintenance of a healthy immune system. Overall, H-MET-SER-OH is a key component in the molecular structure of various biological molecules and is essential for the proper functioning of living organisms.
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 articles and documents
ISOLATION AND CHARACTERIZATION OF AN L-AMINO ACID ACYLASE FROM Aspergillus oryzae
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.