Chemical studies on actinoxanthin.
- 1 January 1976
- journal article
- research article
- Published by Japan Antibiotics Research Association in The Journal of Antibiotics
- Vol. 29 (10) , 1026-1034
- https://doi.org/10.7164/antibiotics.29.1026
Abstract
The antitumor protein actinoxanthin exhibits high inhibitory activity against a number of gram-positive bacteria and some strains of transplantable leukoses and related tumors. Actinoxanthin consists of a single polypeptide chain crosslinked by 2 disulfide bonds and contains 107 amino acid residues. Reduced and alkylated actinoxanthin was digested with chymotrypsin, thermolysin and trypsin. Based on the sequence analysis of fragments so obtained, the complete amino acid sequence and the location of disulfide bonds of actinoxanthin has been proposed. The high degree homology of some regions of actinoxanthin and the antitumor protein neocarzinostatin were revealed.This publication has 4 references indexed in Scilit:
- Critical evaluation of the selective tritiation method of determining C-terminal amino acids and its application to luteinizing hormoneBiochemistry, 1968
- Location of disulphide bridges by diagonal paper electrophoresis. The disulphide bridges of bovine chymotrypsinogen A.Biochemical Journal, 1966
- On the Aminoethylation of ProteinsJournal of Biological Chemistry, 1966
- The Preparation and Enzymatic Hydrolysis of Reduced and S-Carboxymethylated ProteinsJournal of Biological Chemistry, 1963