scholarly journals The amino acid sequence of Clostridium pasteurianum iron protein, a component of nitrogenase. III. The NH2-terminal and COOH-terminal sequences, tryptic peptides of large cyanogen bromide peptides, and the complete sequence.

1977 ◽  
Vol 252 (20) ◽  
pp. 7093-7100
Author(s):  
M Tanaka ◽  
M Haniu ◽  
K T Yasunobu
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Protein A ◽  
Complete Sequence ◽  
Clostridium Pasteurianum ◽  
Tryptic Peptides ◽  
Iron Protein

scholarly journals Amino Acid Sequence of the ß-Chain of the Tetrameric Haemoglobin of the Bivalve Mollusc, Anadara trapezia

1985 ◽  
Vol 38 (3) ◽  
pp. 221 ◽  
Author(s):  
AT Gilbert ◽  
EOP Thompson
Keyword(s):  
Liquid Chromatography ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Peptide Mapping ◽  
Sequence Data ◽  
Bivalve Mollusc ◽  
Tryptic Peptides ◽  
Highperformance Liquid Chromatography ◽  
Additional Sequence

The amino acid sequence of the iJ-chain of the principal haemoglobin from A. trapezia has been determined. The sequence was deduced from the sequences of tryptic peptides, which were fractionated using highperformance liquid chromatography and peptide mapping. Additional sequence data, particularly for the large tryptic peptides, was obtained from enzyme digests of both cyanogen bromide fragments and large citraconyitryptic peptides.

scholarly journals On the Primary Structure of Human Fibrinogen

1977 ◽  
Author(s):  
A. Henschen ◽  
F. Lottspeich ◽  
E. Töpfer-Petersen ◽  
R. Warbinek
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Primary Structure ◽  
Cyanogen Bromide ◽  
Attachment Site ◽  
Complete Sequence ◽  
Cleavage Sites ◽  
Amino Acid Residues ◽  
Human Fibrinogen ◽  
Β Chain

The aim of the present investigation is to elucidate the primary structure of human fibrinogen. Through the work of several laboratories including our own large parts of the structure are now known. Here will be reported the complete amino acid sequence of the γ-chain (409 residues). Furthermore, the carbohydrate linkage site in the β-chain and plasmin cleavage sites in the β- and γ-chains have been identified.The peptide chains were isolated by CM-cellulose chromatography following mercaptolysis and alkylation. The γ-chain was cleaved in a way to produce large fragments suitable for automatic sequencing, e. g. with cyanogen bromide or trypsin after citraconylation. The sequences of the isolated fragments allowed reconstruction of the complete sequence of the γ-chain.The carbohydrate linkage site in the β-chain could be isolated by affinity chromatography on concanavalin A-agarose following cleavage of the chain by trypsin or cyanogen bromide. The sequence of 21 amino acid residues around the carbohydrate attachment site was determined.The plasmin cleavage site giving rise to N-terminal glycine in the γ-chain D-fragment was identified. The amino acid sequence linking plasmic fragments E and D in the β-chain was determined.

scholarly journals The amino acid sequence of Neurospora NADP-specific glutamate dehydrogenase. Peptic and chymotryptic peptides and the complete sequence

1975 ◽  
Vol 149 (3) ◽  
pp. 757-773 ◽  
Author(s):  
A A Holder ◽  
J C Wootton ◽  
A J Baron ◽  
G K Chambers ◽  
J R S. Fincham
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Neurospora Crassa ◽  
Glutamate Dehydrogenase ◽  
Polypeptide Chain ◽  
Complete Sequence ◽  
British Library ◽  
Tryptic Peptides

Peptic and chymotryptic peptides were isolated form the NADP-specific glutamate dehydrogenase of Neurospora crassa and substantially sequenced. Out of 452 residues in the polypeptide chain, 265 were recovered in the peptic and 427 in the chymotryptic peptides. Together with the tryptic peptides [Wootton, J. C., Taylor, J. G., Jackson, A. A., Chambers, G. K. & Fincham, J. R. S. (1975) Biochem. J.149, 749-755], these establish the complete sequence of the chain, including the acid and amide assignments, except for seven places where overlaps are inadequate. These remaining alignments are deduced from information on the CNBr fragments obtained in another laboratory [Blumenthal, K. M., Moon, K. & Smith, E. L. (1975), J. Biol. Chem.250, 3644-3654]. Further information has been deposited as Supplementary Publication SUP 50054 (17 pages) with the British Library (Lending Division), Boston Spa, Wetherby, W. Yorkshire LS23 7BQ, U.K., from whom copies may be obtained under the terms given in Biochem. J. (1975) 145, 5.

scholarly journals Amino Acid Sequence Studies on Sheep Liver Fructose-bisphosphatase. II The Complete Sequence

1983 ◽  
Vol 36 (3) ◽  
pp. 235 ◽  
Author(s):  
WK Fisher ◽  
EOP Thompson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Complete Sequence ◽  
Amino Acid Sequences ◽  
Fructose Bisphosphatase ◽  
Proteolytic Digestion ◽  
Sheep Liver ◽  
Methionine Residues

The cyanogen bromide fragments of S-carboxymethylated fructose-bisphosphatase were purified. The amino acid sequences of the small fragments were determined by the dansyl-Edman method. The large fragments were subjected to proteolytic digestion to give smaller peptides more amenable for purification and sequencing by similar methods. Enzyme digests of the S-carboxymethylated enzyme gave overlap peptides containing the methionine residues.

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