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 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.

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 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.

Die primäre Proteinstruktur von Stämmen des Tabakmosaikvirus

1963 ◽  
Vol 18 (12) ◽  
pp. 1032-1049 ◽  
Author(s):  
B. Wittmann-Liebold ◽  
H. G. Wittmann
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Amino Acid Sequences ◽  
Tryptic Peptides

The amino acid sequence of dahlemense, a naturally occuring strain of tobacco mosaic virus, has been determined and compared with that of the strain vulgare (Fig. 7). In this communication the experimental details are given for the elucidation of the amino acid sequences within two tryptic peptides with 65 amino acids.

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 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.

Die primäre Proteinstruktur von Stämmen des Tabakmosaikvirus

1969 ◽  
Vol 24 (7) ◽  
pp. 877-885 ◽  
Author(s):  
H. G. Wittmann ◽  
I. Hindennach ◽  
B. Wittmann-Liebold
Keyword(s):  
Experimental Data ◽  
Amino Acids ◽  
Amino Acid ◽  
Coat Protein ◽  
Amino Acid Sequence ◽  
Spatial Structure ◽  
Amino Acid Sequences ◽  
The Other ◽  
Tryptic Peptides ◽  
Tmv Strains

Experimental data for determining a) the amino acid sequences of eight tryptic peptides containing 95 amino acids and b) the order of the tryptic peptides are given. Combining the data of this and of a previous paper the complete amino acid sequence of the coat protein of the TMV strain Holmes rib grass (HRG) is established (Fig. 5). It is compared with three other TMV strains the sequences of which have been determined before (Fig. 6).Differences and similarities between the sequences of the four TMV strains are discussed. HRG has a deletion of two amino acids and it is the most distantly related of the four TMV strains. When the sequence of HRG is compared to that of any of the other strains it turns out that in each case more than 50% of the 156 positions contain different amino acids (Fig. 7).The number of positions with the same amino acid in all strains and mutants so far studied is 30 per cent. These positions are not randomly distributed but clustered mainly in two regions. This finding probably reflects the restriction of amino acid exchanges by the spatial structure of the viral rod.

Synopses from the poster exhibition organized by I. M. Kerr, 1. Interferon: a tertiary structure predicted from amino acid sequences

1982 ◽  
Vol 299 (1094) ◽  
pp. 125-127 ◽  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Tertiary Structure ◽  
Three Dimensional ◽  
Amino Acid Sequences ◽  
Dimensional Structure ◽  
X Ray ◽  
Three Dimensional Structure ◽  
X Ray Crystallography ◽  
Functional Studies

Functional studies on interferon would be helped by a three-dimensional structure for the molecule. However, it may be several years before the structure of the protein is determined by X-ray crystallography. We have therefore used available methods for predicting the secondary - and the tertiary - structure of a protein from its amino acid sequence to propose a tertiary model involving the packing of four a-helices. Details of this work have been published elsewhere (Sternberg & Cohen 1982).

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