Gramicidin S: the sequence of the amino-acid residues

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منابع مشابه

Gramicidin S; the sequence of the amino-acid residues.

Consden, R., Gordon, A. H. & Martin, A. J. P. (1944). Biochem. J. 38, 224. Consden, R., Gordon, A. H. & Martin, A. J. P. (1945). Biochem. J. 39, xlvi. Consden, R., Gordon, A. H. & Martin, A. J. P. (1946a). Biochem. J. 40, 33. Consden, R., Gordon, A. H. & Martin, A. J. P. (1946b). Biochem. J. 40, 580. Consden, R., Gordon, A. H., Martin, A. J. P. & Synge, R. L. M. (1947). Biochem. J. 41, 596. Mar...

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The free amino group of gramicidin S.

on the other hand, maintain that both amino and carboxyl groups are present and that the 8-amino group of the ornithine residue is not free. Their evidence for this latter point, nevertheless, is not very convincing and the problem was clearly one which could be readily settled by applying the new dinitrofluorobenzene (DNFB) method (Sanger, 1945). Accordingly at Dr Synge's suggestion, the prese...

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The sequence of the amino acid residues in performic acid-oxidized ribonuclease.

In previous studies (3) a partial structural formula for oxidized bovine ribonuclease was derived from knowledge of the peptides formed by the action of trypsin (4), chymotrypsin (3), and pepsin (5). The results showed the order in which the peptides were linked to one another to form the single peptide chain of 124 amino acid residues present in the parent molecule. The preparation of milligra...

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The Sequence of the Amino Acid Residues in Performic Acid-oxidized Ribonuclease*

In previous studies (3) a partial structural formula for oxidized bovine ribonuclease was derived from knowledge of the peptides formed by the action of trypsin (4), chymotrypsin (3), and pepsin (5). The results showed the order in which the peptides were linked to one another to form the single peptide chain of 124 amino acid residues present in the parent molecule. The preparation of milligra...

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Human parathyroid hormone: amino-acid sequence of the amino-terminal residues 1-34.

Human parathyroid hormone has been isolated in highly purified form from human parathyroid adenomas. The primary sequence of the amino-terminal 34 residues of the human hormone was obtained by automated degradation with a Beckman Sequencer. The phenylthiohydantoin amino acids were identified by gas chromatography and mass spectrometry. The first 34 residues of human parathyroid hormone differ f...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1947

ISSN: 0306-3283

DOI: 10.1042/bj0410596