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 Amino Acid Sequence of the Globin lIB Chain of the Dimeric Haemoglobin of the Bivalve Mollusc Andara trapezia

1984 ◽  
Vol 37 (4) ◽  
pp. 191 ◽  
Author(s):  
WK Fisher ◽  
AT Gilbert ◽  
EOP Thompson
Keyword(s):  
High Performance Liquid Chromatography ◽  
Liquid Chromatography ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
High Performance ◽  
Bivalve Mollusc ◽  
Amino Acid Sequences ◽  
Globin Chain ◽  
Tryptic Peptides

The tryptic peptides of the S-carboxymethylated globin chain ofa dimeric haemoglobin from A. trapezia were purified by high-performance liquid chromatography and their amino acid sequences determined by the dansyl-Edman method.

scholarly journals The amino acid sequence of the α chain of the major haemoglobin of the rat (Rattus norvegicus)

1975 ◽  
Vol 149 (1) ◽  
pp. 259-269 ◽  
Author(s):  
C G Chua ◽  
R W Carrell ◽  
B H Howard
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Rattus Norvegicus ◽  
Peptide Mapping ◽  
Cysteine Residue ◽  
British Library ◽  
Peptide Fragments ◽  
Partial Amino Acid Sequence ◽  
Tryptic Peptides ◽  
Α Chain

1. A partial amino acid sequence of the α chain from the rat (Wistar, Rattus norvegicus) major haemoglobin is reported. The soluble tryptic peptides prepared from aminoethylated α-globin were separated by peptide ‘mapping’. Sequencing of the tryptic peptides was carried out by the dansyl-Edman method and by the overlapping of smaller peptide fragments derived from secondary enzymic digestion. The insoluble ‘core’ peptides were further digested with chymotrypsin, thermolysin and pepsin to give smaller soluble peptides for sequencing. The tryptic peptides were ordered on the basis of their homology with the corresponding peptides of human α chain. 2. The proposed sequence is compared with that obtained by using an automated sequencer [Garrick et al. (1975) Biochem. J.149, 245-258]. The differences in sequence resulting from the two methods are discussed. 3. It is suggested that the externally situated cysteine (residue 13) is responsible for the observed inhibition of crystallization of rat haemoglobin at alkaline pH. 4. Detailed evidence for the sequence has been deposited as Supplementary Publication SUP 50047 (9 pages) at the British Library (Linding Division), Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from which copies can be obtained on the terms given in Biochem. J. (1975) 145, 5.

scholarly journals Amino Acid Sequence Studies on the γ-Chain of Human Fibrinogen

1977 ◽  
Author(s):  
H. Bouma ◽  
B. A. Cottrell ◽  
S. J. Friezner ◽  
T. Takagi ◽  
R. F. Doolittle
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Sequence Data ◽  
Structural Features ◽  
Tryptic Digestion ◽  
Cysteine Residues ◽  
Human Fibrinogen

The γ-chain of human fibrinogen contains 400±10 residues, eight of which are methionines. As such, we have isolated and characterized nine cyanogen bromide peptides. The alignment of these fragments was attained by the isolation of key overlap peptides derived from the tryptic digestion of citraconylated γ-chains and succinylated and aminoethylated γ-chains. In the latter case we synthesized a radioactive aminoethylating agent which was especially useful in isolating all the cysteine-containing peptides. The amino acid sequence of most of these fragments has been accomplished by a variety of procedures. In general, our results are in harmony with those recently reported by Henschen et al. (Hoppe-Seyler’s Z. Physiol. Chem., 357, 605, 1976), although some differences exist.The most interesting structural features revealed by the sequence data include significant homologies with the α- and β-chains, especially with regard to the arrangement of certain key cysteine residues. Thus, the sequence at residues γ 135–139 is Cys-Gln-Glu-Pro-Cys, in striking parallel with the sequence at residues γ 19–23, which is Cys-Pro-Thr-Thr-Cys. The occurrence of similar pentapeptide skeins in the α- and β-chains, in each case separated by about the same number of residues, has both structural and evolutionary connotations.

The primary structure of staphylococcal protease

1978 ◽  
Vol 56 (6) ◽  
pp. 534-544 ◽  
Author(s):  
Gabriel R. Drapeau
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Primary Structure ◽  
Serine Proteases ◽  
Cyanogen Bromide ◽  
Streptomyces Griseus ◽  
Tryptic Peptides ◽  
Single Polypeptide Chain ◽  
Sequence Homologies ◽  
Single Polypeptide

The amino acid sequence of staphylococcal protease has been determined by analysis of tryptic peptides obtained from cyanogen bromide fragments. Selected peptides obtained from digests with staphylococcal protease, thermolysin, and chymotrypsin provided the information necessary to align the tryptic peptides and the cyanogen bromide fragments. The protease is a single polypeptide chain of some 250 amino acids and is devoid of sulfhydryl groups. The COOH-terminal tryptic peptide of the protease molecule contains some 43 residues, most of which are aspartic acids, asparagines, and prolines. The amino acid sequence of this peptide was not determined. The primary structure near the active serine residue indicates that staphylococcal protease is related to the pancreatic serine proteases. However, it has little or no additional sequence homologies with these enzymes except for the regions near histidine-50 and aspartic acid - 91. These regions have striking similarities with the corresponding regions of protease B and the trypsin-like enzyme of Streptomyces griseus.

Amino acid sequence of cyanogen bromide fragment CB3 of hog pepsin

1981 ◽  
Vol 46 (3) ◽  
pp. 655-666
Author(s):  
Ladislav Morávek ◽  
Vladimír Kostka
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Methionine Residues ◽  
Cyanogen Bromide Fragment

On the basis of the knowlidge of thermolytic, chymotryptic and substilisin peptides the amino acid sequence was determined of cyanogen bromide fragment CB3 representing the region between methionine residues I and II of pepsin: Thr-Gly-Ile-Leu-Gly-Tyr-Asp-Thr-Val-Gln-Val-Gly-Gly-Ile-Ser-Asp-Thr-Asn-Gln-Ile-Phe-Gly-Leu-Ser-Glu-Thr-Glu-Pro-Gly-Ser-Phe-Leu-Tyr-Tyr-Ala-Pro-Phe-Asp-Gly-Ile-Leu-Gly-Leu-Ala-Tyr-Pro-Ser-Ile-Ser-Ala-Ser-Gly-Ala-Thr-Pro-Val-Phe-Asp-Asn-Leu-Trp-Asp-Gln-Gly-Leu-Val-Ser-Gln-Asp-Leu-Phe-Ser-Val-Tyr-Leu-Ser-Ser-Asn-Asp-Asp-Ser-Gly-Ser-Val-Val-Leu-Leu-Gly-Gly-Ile-Asp-Ser-Ser-Tyr-Tyr-Thr-Gly-Ser-Leu-Asn-Trp-Val-Pro-Val-Ser-Val-Glu-Gly-Tyr-Trp-Gln-Ile-Thr-Leu-Asp-Ser-Ile-Thr-Met.

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