Alpha Sarcin, a New Antitumor Agent: I. Isolation, Purification, Chemical Composition, and the Identity of a New Amino Acid
AUTOR(ES)
Olson, B. H.
RESUMO
Isolation and purification procedures are given for the new antitumor agent, alpha sarcin. These procedures include the use of column ion exchange with a carboxylic resin (Amberlite IRC50), dialysis, decolorization with activated charcoal, gradient salt chromatography, salt removal, and drying from the frozen state. The final product has an activity of 800 sarcoma 180 mouse dilution units per mg. The amino acid composition of the purified material is reported. All of the usual amino acids found in proteins were present except methionine. In addition to the usual amino acids, an unknown amino acid was present in the acid hydrolysate. The latter was isolated, and was found to yield phenylalanine and kynurenine. This compound, which has been named “sarcinine,” is extremely stable in 6 n hydrochloric acid in the absence of air, and is unstable in alkali. Sarcinine has also been found in two other antitumor peptides produced by aspergilli, and so may relate significantly to the antitumor properties of these peptides.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1058250Documentos Relacionados
- Alpha Sarcin, a New Antitumor Agent: II. Fermentation and Antitumor Spectrum
- A New Bacterial Agglutinin from Soybean: I. ISOLATION, PARTIAL PURIFICATION, AND CHARACTERIZATION 1
- STUDIES OF STREPTOCOCCAL CELL WALLS I. : Isolation, Chemical Composition, and Preparation of m Protein1
- ACETYLCHOLINESTERASE, I. LARGE-SCALE PURIFICATION, HOMOGENEITY, AND AMINO ACID ANALYSIS*
- Malate dehydrogenase from the thermophilic green bacterium Chloroflexus aurantiacus: purification, molecular weight, amino acid composition, and partial amino acid sequence.
