The Complete Amino Acid Sequences of Both Subunits of the Sweet Protein Monellin
- 1 January 1976
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 357 (1) , 585-592
- https://doi.org/10.1515/bchm2.1976.357.1.585
Abstract
The amino acid sequences of both chains of the sweet protein Monellin [Dioscoreophyllum cuminsii] were determined. Since chain separation could not be accomplished easily, cyanogen bromide cleavage at the only methionine residue (in the B-chain) was performed and the 3 products obtained were separated. For the identification of amino acid phenylthiohydantoins, high performance liquid chromatography was employed. Thus 37 out of a total of 44 residues of the A chain and 40 out of a total of 42 residues of the large CNBr fragment of the B chain could be determined after Edman degradation of the polypeptides on an automated sequenator.This publication has 5 references indexed in Scilit:
- The structure of monellin and its relation to the sweetness of the proteinBiochimica et Biophysica Acta (BBA) - Protein Structure, 1976
- Crystallization and Crystal Data of MonellinProceedings of the National Academy of Sciences, 1975
- Nonenzymatic Cleavage of Peptide Bonds: The Methionine Residues in Bovine Pancreatic RibonucleaseJournal of Biological Chemistry, 1962