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 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.

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.

Carnivora: The Amino Acid Sequence of the Adult European Polecat (Mustela putorius, Mustelidae) Hemoglobins

1989 ◽  
Vol 44 (7) ◽  
pp. 817-824 ◽  
Author(s):  
Aftab Ahmed ◽  
Meeno Jahan ◽  
Gerhard Braunitzer ◽  
Helmut Pechlaner
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Gas Phase ◽  
Primary Structure ◽  
Amino Acid Sequences ◽  
Mustela Putorius ◽  
Globin Chains ◽  
The Family ◽  
High Degree ◽  
Β Chain

The complete amino acid sequences of the hemoglobins from the adult European polecat (Mustela putorius) are presented. The erythrocytes contain two hemoglobin components and three globin chains (α I, α II and β). The primary structure of globin chains and of the tryptic peptides determined in liquid- and gas-phase sequantors. Comparing the sequences of the globin chains of the polecat with that of human Hb-A, 17 (23.9%) substitutions were recognized in the α I, 16 (22.5%) in the α II and 14 (20.4%) in the β chain. A high degree of homology observed with other representatives of the family Mustelidae.

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.

Amino Acid Sequences in All Soluble Tryptic Peptides from β-Chain of Macaca mulatta Monkey Hemoglobin

1968 ◽  
Vol 63 (1) ◽  
pp. 136-137 ◽  
Author(s):  
GENJI MATSUDA ◽  
TETSUO MAITA ◽  
MASATO YAMAGUCHI ◽  
HISAHIRO OTA ◽  
MASAHARU MIGITA ◽  
...  
Keyword(s):  
Amino Acid ◽  
Macaca Mulatta ◽  
Amino Acid Sequences ◽  
Tryptic Peptides ◽  
Β Chain

Gene action in the human haptoglobins. IV. Amino acid sequence studies on the haptoglobin α chains

1970 ◽  
Vol 48 (1) ◽  
pp. 133-146 ◽  
Author(s):  
J. A. Black ◽  
G. H. Dixon
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Amino Acid Sequences ◽  
Dansyl Amino Acids ◽  
Tryptic Peptides ◽  
Specific Chemical ◽  
Chloromethyl Ketone ◽  
Partial Gene Duplication ◽  
Arginyl Residues

Alpha chains of human haptoglobin have been prepared from whole haptoglobin of genetic type Hp 2–1 purified from the ascites fluid of a single patient. Amino acid sequence analysis has been carried out on these light chains which represent the products α1S and α2(F,S) of the single genes Hp1S and Hp2(F,S), and are, respectively, 83 and 142 residues in length. The data reported here concern the sequence analysis of two series of tryptic peptides, one obtained by unlimited cleavage of the chains by p-toluene sulfonamido-phenylethyl chloromethyl ketone - trypsin, and the second following limitation of trypsin cleavage to arginyl residues after modification of lysyl residues by trifluoracetylation. The major technique for sequence analysis of these peptides was a modification of the p-dimethylaminonaphthalene-sulfonyl-Edman (dansyl-Edman) procedure employing a new thin-layer chromatographic separation of the dansyl-amino acids. The sequences of these tryptic peptides in conjunction with those of the chymotryptic peptides allowed the unequivocal deduction of portions of the sequence, but the final overlaps were provided by fragments obtained by specific chemical cleavage of the chain at aspartyl residues. The amino acid sequences deduced have documented the occurrence of a partial gene duplication in the gene product α2(F,S) of the Hp2(F,S) gene.

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 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.

Sign in / Sign up

Export Citation Format

Share Document