Isolation of Tryptic Peptides from the lie Chain of Ricin D and the Sequences of Some Tryptic Peptides Including N- and C-Terminal Peptides
- 1 July 1977
- journal article
- research article
- Published by Oxford University Press (OUP) in Agricultural and Biological Chemistry
- Vol. 41 (7) , 1225-1231
- https://doi.org/10.1080/00021369.1977.10862650
Abstract
Twenty tryptic peptides were isolated from the performic acid-oxidized He chain of ricin D by Dowex 1 × 2 column chromatography followed by paper chromatography. The amino acids contained in these peptides accounted for 218 out of 266 residues in the whole protein. The amino acid sequences of nine peptides were determined by manual liquid phase or automatic solid phase Edman degradation, and N- and C-terminal sequences of the He chain of ricin D were established to be NH2–Ile–Phe–Pro–Lys–Gln–Tyr–Pro–Ile–Ile– and Cys–Ala–Pro–Pro–Pro–Ser–Ser–Gln–Phe, respectively.This publication has 4 references indexed in Scilit:
- Separation of the Two Constituent Polypeptide Chains of Ricin DAgricultural and Biological Chemistry, 1977
- The Mode of Binding of Carbohydrate in Ricin DAgricultural and Biological Chemistry, 1975
- Studies on the Amino Acid Sequence of Holmes Rib-Grass Strain Virus ProteinAgricultural and Biological Chemistry, 1967
- Separation of Tryptic Peptides of Tobacco Mosaic Virus and Strain Proteins by an Improved Method of Column Chromatography*Biochemistry, 1964