The Complete Amino Acid Sequences of Both Subunits of the Sweet Protein Monellin

The Complete Amino Acid Sequences of Both Subunits of the Sweet Protein Monellin Hoppe-Seyler's Z. Physiol. Chem. Bd. 357, S. 585 - 592, Aprü 1976 Gerhard FRANK and Herbert ZUBER Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule Zürich-Hönggerberg (Received 29 January 1976) Summary: The amino acid sequences of both chains of the sweet protein Monellin have been 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 three products obtained after cyanogen bromide cleavage were separated. For the identification of amino acid phenylthio- hydantoins, 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. Die vollständige Aminosäure-Sequenz der beiden Ketten des süßen Proteins Monellin Zusammenfassung: Die Aminosäuresequenz beider Ketten des süßen Proteins Monellin wurde ermittelt. Da eine Kettentrennung nicht leicht erreicht werden konnte, wurde eine Bromcyanspaltung an dem einzigen Methioninrest (in der B-Kette) durchgeführt und die drei nach der Bromcyanspaltung erhaltenen Produkte wurden getrennt. Zur Identifizierung der Aminosäure-PhenylthioMonellin, the sweet principle of Dioscoreophyllum cuminsii, is a http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png hoppe-seyler's zeitschrift für physiologische chemie de Gruyter

The Complete Amino Acid Sequences of Both Subunits of the Sweet Protein Monellin

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Publisher
de Gruyter
Copyright
Copyright © 1976 by the
ISSN
0018-4888
eISSN
1437-4315
DOI
10.1515/bchm2.1976.357.1.585
Publisher site
See Article on Publisher Site

Abstract

Hoppe-Seyler's Z. Physiol. Chem. Bd. 357, S. 585 - 592, Aprü 1976 Gerhard FRANK and Herbert ZUBER Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule Zürich-Hönggerberg (Received 29 January 1976) Summary: The amino acid sequences of both chains of the sweet protein Monellin have been 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 three products obtained after cyanogen bromide cleavage were separated. For the identification of amino acid phenylthio- hydantoins, 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. Die vollständige Aminosäure-Sequenz der beiden Ketten des süßen Proteins Monellin Zusammenfassung: Die Aminosäuresequenz beider Ketten des süßen Proteins Monellin wurde ermittelt. Da eine Kettentrennung nicht leicht erreicht werden konnte, wurde eine Bromcyanspaltung an dem einzigen Methioninrest (in der B-Kette) durchgeführt und die drei nach der Bromcyanspaltung erhaltenen Produkte wurden getrennt. Zur Identifizierung der Aminosäure-PhenylthioMonellin, the sweet principle of Dioscoreophyllum cuminsii, is a

Journal

hoppe-seyler's zeitschrift für physiologische chemiede Gruyter

Published: Jan 1, 1976

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