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 The amino acid sequence of Neurospora NADP-specific glutamate dehydrogenase. The tryptic peptides

1975 ◽  
Vol 149 (3) ◽  
pp. 739-748 ◽  
Author(s):  
J C Wootton ◽  
J G Taylor ◽  
A A Jackson ◽  
G K Chambers ◽  
J R S. Fincham
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Neurospora Crassa ◽  
Glutamate Dehydrogenase ◽  
Polypeptide Chain ◽  
British Library ◽  
Tryptic Peptides

The NADP-specific glutamate dehydrogenase of Neurospora crassa was digested with trypsin, and peptides accounting for 441 out of the 452 residues of the polypeptide chain were isolated and substantially sequenced. Additional experimental detail has been deposited as Supplementary Publication SUP 50052 (11 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 The amino acid sequence of the tryptic peptides from actinidin, a proteolytic enzyme from the fruit of Actinidia chinensis

1978 ◽  
Vol 173 (1) ◽  
pp. 73-83 ◽  
Author(s):  
A Carne ◽  
C H Moore
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Proteolytic Enzyme ◽  
Polypeptide Chain ◽  
Amino Acid Sequences ◽  
British Library ◽  
Actinidia Chinensis ◽  
Tryptic Peptides ◽  
X Ray ◽  
Thiol Proteinase

The amino acid sequences of the tryptic peptides of the thiol proteinase actinidin from Actinidia chinensis were determined by the manual dansyl–Edman procedure. There are 12 tryptic peptides, which give a polypeptide chain of 220 residues with a mol.wt. of 23500. An alignment of the tryptic peptides was made by using the X-ray-crystallographic data of Baker [(1977) J. Mol. Biol. 115, 263–277] determined at 0.28 nm resolution on crystalline actinidin. Detailed evidence for the amino acid sequences of the tryptic peptides has been deposited as Supplementary Publication SUP 50083 (14 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1978) 169, 5.

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 of NADP-Specific Glutamate Dehydrogenase of Neurospora crassa

1974 ◽  
Vol 71 (11) ◽  
pp. 4361-4365 ◽  
Author(s):  
J. C. Wootton ◽  
G. K. Chambers ◽  
A. A. Holder ◽  
A. J. Baron ◽  
J. G. Taylor ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Neurospora Crassa ◽  
Glutamate Dehydrogenase

scholarly journals A collagen-like amino acid sequence in a polypeptide chain of human C1q (a subcomponent of the first component of complement)

1974 ◽  
Vol 141 (1) ◽  
pp. 189-203 ◽  
Author(s):  
Kenneth B. M. Reid
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Polypeptide Chain ◽  
Complete Sequence ◽  
Partial Amino Acid Sequence ◽  
Collagenase Digestion ◽  
A Chain

1. A partial amino acid sequence of 95 residues of the 191 residues in the oxidized A chain of human subcomponent C1q was determined. The partial nature of the sequence is because one overlapping peptide is missing in the proposed sequence, also the proof of some of the overlapping peptides depends partly on their amino acid composition and not on their complete sequence. 2. This region of the A chain contained a repeating sequence of glycine-X-Y (where X is often proline and Y is often hydroxyproline) for 78 residues. 3. The five hydroxylysine residues and the five hydroxyproline residues present in the oxidized A chain were all in these 78 residues and only in the Y position of the repeating sequence. 4. Prolonged collagenase digestion of the oxidized A chain yielded a large, apparently C-terminal, peptide which contained most of the non-collagenous sequences present in the chain. 5. It is concluded that there is a collagen-like region in the A chain of subcomponent C1q which constitutes most of the N-terminal half of the chain and that similar collagen-like regions will be found in the B and C chains.

Amino acid sequences of some tryptic peptides from the β-chain of horse hemoglobin

1968 ◽  
Vol 46 (8) ◽  
pp. 825-843 ◽  
Author(s):  
David B. Smith
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Polypeptide Chain ◽  
Amino Acid Sequences ◽  
Human Hemoglobin ◽  
Tryptic Peptides ◽  
Chain Sequence ◽  
Β Chain

Evidence for the amino acid sequence of some peptides formed by the action of trypsin on the β-polypeptide chain of horse hemoglobin is presented. By analogy with the amino acid sequence of the β-chain of human hemoglobin, these peptides cover positions 1 to 82 and 117 to 146 of the horse β-chain. Twenty-one differences between the human and horse β-chain sequence are found in these regions.

scholarly journals Neurotoxins from the venoms of the sea snakes Hydrophis ornatus and Hydrophis lapemoides

1983 ◽  
Vol 213 (1) ◽  
pp. 31-38 ◽  
Author(s):  
N Tamiya ◽  
N Maeda ◽  
H G Cogger
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Paper Electrophoresis ◽  
Amino Acid Sequences ◽  
British Library ◽  
Amino Acid Residues ◽  
Protein Amino Acid ◽  
Tryptic Peptides ◽  
Sea Snakes ◽  
And Migration

The main neurotoxic components, toxins Hydrophis ornatus a and Hydrophis lapemoides a, were isolated from the venoms of the sea snakes Hydrophis ornatus and Hydrophis lapemoides respectively. The amino acid sequence of toxin Hydrophis ornatus a was deduced to be identical with that of toxin Astrotia stokesii a [Maeda & Tamiya (1978) Biochem. J. 175, 507-517] on the basis of identity of the tryptic peptide ‘map’ and the amino acid composition of each peptide. The amino acid sequence of toxin Hydrophis lapemoides a was determined mainly on the basis of identity of the amino acid compositions, mobilities on paper electrophoresis and migration positions on paper chromatography of the tryptic peptides with those of other sea-snake toxins whose sequences are known. Both toxins Hydrophis ornatus a and Hydrophis lapemoides a consisted of 60 amino acid residues and there were six amino acid replacements between them. The taxonomy of sea snakes in the Hydrophis ornatus complex has long been confused, and the above snakes were originally assigned to taxa that proved to be inconsistent with the relationships indicated by the neurotoxin amino acid sequences obtained. A subsequent re-examination of the specimens revealed an error in the original identifications and demonstrated the value of the protein amino acid sequences in systematic and phylogenetic studies. The isolation procedure and results of amino acid analysis of the tryptic peptides have been deposited as Supplementary Publication SUP 50121 (8 pages) with the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies may be obtained as indicated in Biochem. J. (1983) 209, 5.

scholarly journals The amino acid sequence of the cytochrome c-554(547) from the chemolithotrophic bacterium Thiobacillus neapolitanus

1985 ◽  
Vol 227 (3) ◽  
pp. 1009-1013 ◽  
Author(s):  
R P Ambler ◽  
T E Meyer ◽  
P A Trudinger ◽  
M D Kamen
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Polypeptide Chain ◽  
Cysteine Residues ◽  
British Library ◽  
Thiobacillus Neapolitanus

An amino acid sequence is proposed for the cytochrome c-554(547) from the bacterium Thiobacillus neapolitanus N.C.I.B. 8539). It consists of a polypeptide chain of 91 residues, with a pair of haem-attachment cysteine residues at positions 15 and 18. There is similarity in sequence with each of the halves of the sequence of the dihaem cytochromes c4 and with a cytochrome c-554(548) from a halophilic strain of Paracoccus. Detailed evidence for the amino acid sequence of the protein has been deposited as Supplementary Publication SUP 50127 (11 pages) at the British Library (Lending Division), Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1985) 225, 5.

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