Isolation of Glycopeptides from Ricin D
- 1 August 1975
- journal article
- research article
- Published by Oxford University Press (OUP) in Agricultural and Biological Chemistry
- Vol. 39 (8) , 1645-1650
- https://doi.org/10.1080/00021369.1975.10861828
Abstract
Ricin D, a toxic protein from castor bean (Ricinus communis), contained 6 moles of glucosamine and 17 moles of mannose per mole of protein. Isolation of 2 constituent polypeptide chains, namely Ala-chain and Ile-chain, and subsequent proteolytic digestions with Nagarse and Pronase revealed 2 glycopeptides (Asp1 Thr1 Gly1 glucosamine2 mannose6 and Asp1 Thr1 Glu1 Pro1 glucosamine2 mannose7) from Ala-chain and one (Asp1 Ile1 Phe1 glucosamine2 mannose4) from Ile-chain. The total carbohydrate content of these glycopeptides accounts for all that of the whole protein. Carbohydrate moieties are covalently linked to the polypeptide chains in 3 sites to form this glycoprotein.This publication has 2 references indexed in Scilit:
- The Mode of Binding of Carbohydrate in Ricin DAgricultural and Biological Chemistry, 1975
- DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*Annals of the New York Academy of Sciences, 1964