Separation of the Two Constituent Polypeptide Chains of Ricin D
- 1 July 1977
- journal article
- research article
- Published by Oxford University Press (OUP) in Agricultural and Biological Chemistry
- Vol. 41 (7) , 1211-1215
- https://doi.org/10.1080/00021369.1977.10862648
Abstract
Two constituent polypeptide chains were isolated from performic acid-oxidized ricin D by DEAE-cellulose column chromatography in phosphate buffer, pH 7.0, containing 8m urea or from reduced-carboxymethylated ricin D by gel filtration on Sephadex G-75 followed by DEAE- cellulose column chromatography in Tris-HCl buffer, pH 8.5. Amino acid analyses of the isolated two chains revealed that they were distinct molecules possessing similar molecular weights of near 30,000 and linked by one disulfide bond in ricin D.This publication has 2 references indexed in Scilit:
- The Preparation and Enzymatic Hydrolysis of Reduced and S-Carboxymethylated ProteinsJournal of Biological Chemistry, 1963
- THE OXIDATION OF RIBONUCLEASE WITH PERFORMIC ACIDJournal of Biological Chemistry, 1956