## o-Hydro~y-DL-phenylalanine-2-~~C was prepared by the condensation of o-methoxybenzyl chloride and ethyl acetamidocyano-~c e t a t e -2 -~~C and subsequent hydrolysis. The rucemute was resolved by the stereospecijic action of chymotrypsin on the amino acid ethyl ester at pH 5.0 to give the two i
Radiochromatographic resolution of [14C]DL-tryptophan, [14C]DL-phenylalanine and [35S]DL-methionine on a cellulose column
β Scribed by M. Isoyama; T. Fukuhara; M. Tanaka; A. Shimada; S. Yuasa
- Publisher
- Elsevier Science
- Year
- 1989
- Weight
- 236 KB
- Volume
- 40
- Category
- Article
- ISSN
- 0883-2889
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β¦ Synopsis
[14C]
DL-phenylalanine and [35S]DL-methionine were resolved using cellulose column chromatography. The assignment for the resolved enantiomers was carried out by means of co-chromatography with non-labeled oL-amino acids after modification with fluorodinitrobenzene. The optical purity of the enantiomers was estimated to be greater than 99%. The resolved enantiomers were provided for bioassay, showing that the enantiomer was biochemically active.
π SIMILAR VOLUMES
We have studied the resolution of DL-amino acids on a native cellulose column. All the DL-amino acids related to protein and their 16 DNP-DL-amino acids were separated. The resolution capability depends mainly upon the bulkiness of the side group attached to the β£-carbon, but also on structural and