منابع مشابه
Complete amino acid sequence of the sweet protein monellin.
The sweet protein monellin consists of two noncovalently associated polypeptide chains, the A chain of 44 amino acid residues and the B chain of 50 residues. Two different primary structures have been reported for each of these chains. The complete amino acid sequence of monellin was determined by a combination of FAB- and ESI-mass spectrometry, and by automatic Edman degradation.
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Cyanogen bromide treatment of reduced, S-carboxymethylated phosphoglycerate kinase yielded 14 major peptides, CNBr-1 (20 residues), CNBr-2 (8 residues), CNBr-3 (33 residues), CNBr-4 (11 residues), CNBr-5 (104 residues), CNBr-6 (14 residues), CNBr-7 (37 residues), CNBr-8 (7 residues), CNBr-9 (6 residues), CNBr-10 (11 residues), CNBr-11 (19 residues), CNBr-12 (42 residues), CNBr-13 (44 residues),...
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The active cysteine of papain was labeled with W-iodoacetate and the cystine residues were reduced and coupled with unlabeled iodoacetate. The heptacarboxymethyl papain was then maleylated and hydrolyzed with trypsin. Key peptides were isolated from this hydrolysate which have permitted completion of the amino acid sequence of the protein. Thus, an earlier tentative and incomplete version of th...
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Background and Aims: Since 1998, Iranian poultry industry has been affected by avian influenza (AI) virus, subtype H9N2. The association of high mortality and case report of H5N1 and H9N2 influenza virus in wild birds in recent years raised the suspicion of a possible new genetic modified AI virus. Methods: Partial nucleotide sequences and deduced amino acid of hemagglutinin (HA) genes of 4 H9...
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In a previous paper data were presented that permitted the linear arrangement of five fragments produced by cleavage of an extracellular nuclease of Staphylococcus aureus with cyanogen bromide (1). The amino acid sequences of the tryptic peptides prepared from these fragments, together with the partial sequences of chymotryptic peptides isolated from digests of the intact nuclease, have also be...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1988
ISSN: 0014-5793
DOI: 10.1016/0014-5793(88)81275-4