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1241677-43-9

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1241677-43-9 Usage

General Description

2,3-Dichloro-D-Phenylalanine is a chemical compound that consists of a phenylalanine molecule with two chlorine atoms attached to the 2 and 3 positions on the benzene ring. It is a derivative of the amino acid phenylalanine and is commonly used in the synthesis of pharmaceuticals and agrochemicals. 2,3-Dichloro-D-Phenylalanine has been found to possess antimicrobial and antifungal properties, making it a valuable ingredient in the development of new drugs. Additionally, it has been studied for its potential use in the treatment of cancer and as a building block for the synthesis of novel peptidomimetics. Overall, 2,3-Dichloro-D-Phenylalanine is a versatile compound with potential applications in various fields of research and development.

Check Digit Verification of cas no

The CAS Registry Mumber 1241677-43-9 includes 10 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 7 digits, 1,2,4,1,6,7 and 7 respectively; the second part has 2 digits, 4 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 1241677-43:
(9*1)+(8*2)+(7*4)+(6*1)+(5*6)+(4*7)+(3*7)+(2*4)+(1*3)=149
149 % 10 = 9
So 1241677-43-9 is a valid CAS Registry Number.

1241677-43-9Upstream product

1241677-43-9Downstream Products

1241677-43-9Relevant articles and documents

METABOLISM OF D,L-CHLORO-PHENYLALANINES BY PHENYLALANINE AMINOTRANSFERASE ISOZYMES PURIFIED FROM BUSHBEAN SHOOTS

Taylor, David C.,Wightman, Frank

, p. 1279 - 1288 (2007/10/02)

Key Word Index - Phaseolus vulgaris; Leguminosae; bushbean; metabolism; phenylalanine decarboxylase; phenylalanine aminotransferase; purification; substituted amino acids; D,L-chloro-phenylalanines.A series of mono-, di- and trichloro-D,L-phenylalanines was tested as substrates for both phenylalanine aminotransferase and phenylalanine decarboxylase partially purified from bushbean (Phaseolus vulgaris L.) seedling extracts by ammonium sulphate fractionation and Sephacryl S-300 gel filtration.While most of the D,L-chlorophenylalanines were transaminated at rates of 35-100percent of that observed with D,L-phenylalanine, no chloro-phenylalanine decarboxylase activity was observed.A transamination reaction is therefore likely to be the initial step in the conversion of chloro-phenylalanines to their corresponding chloro-phenylacetic acids via a reaction pathway similar to the known route for the metabolism of L-phenylalanine to phenylacetic acid.The highest specific activity of phenylalanine aminotransferase was found in both root and shoot tissues of bushbean at the 10-day stage of seedling growth.Partially purified extracts of these tissues were able to transaminate most of the mono- and dichloro-phenylalanines at ca 20-40percent of the rate observed with D,L-phenylalanine, while the trichloro-phenylalanines (assayed at lower concentrations due to solubility) were transaminated at rates equal to those observed with D,L-phenylalanine.The 4-chloro derivative was the best substrate tested showing rates of transamination that were 25percent higher than those observed with D,L-phenylalanine.Further purification of shoot fractions by DEAE-Sephacel chromatography resolved the phenylalanine aminotransferase activity into two peaks (enzymes I and II) which on further purification, were found to behave differently during hydrophobic chromatography and PAGE.These results indicated the presence of two isozymic forms of phenylalanine aminotransferase in bushbean shoots and both were found to catalyse transamination of the monochloro-phenylalanines examined in this study.

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