scholarly journals Studies on Monotreme Proteins. VI. Amino Acid Sequence of the ß-Chain of Haemoglobin From the Platypus, Ornithorhynchus anatinus

1975 ◽  
Vol 28 (4) ◽  
pp. 353 ◽  
Author(s):  
RG Whittaker ◽  
EOP Thompson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Sequences ◽  
Tryptic Digestion ◽  
Tryptic Peptides ◽  
Ornithorhynchus Anatinus

The amino acid sequence of the 146 residues of the p-chain of the major haemoglobin from the platypus has been determined. The soluble peptides derived from the chain by tryptic digestion were isolated by paper ionophoresis and chromatography. The amino acid sequences were determined by the dansyl-Edman procedure or by further digestion with other enzymes. The tryptic peptides were aligned by homology with other p-globins. There were 14 changes in sequence compared with echidna p-chain.

scholarly journals Studies on Monotreme Proteins. V. Amino Acid Sequence of the a-Chain of Haemoglobin From the Platypus, Ornithorhynchus anatinus

1974 ◽  
Vol 27 (6) ◽  
pp. 591 ◽  
Author(s):  
RG Whittaker ◽  
EOP Thompson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Sequences ◽  
Tryptic Digestion ◽  
Complete Amino Acid Sequence ◽  
Ornithorhynchus Anatinus ◽  
A Chain

Blood from the platypus contained three haemoglobins which were separated by chromatography on DEAE-Sephadex. The major component, Hb-I, was converted to globin and fractionated into the oc-and p-chains by chromatography on eM-cellulose in 8M urea-thiol buffers, and the complete amino acid sequence of the 141 residues of the oc-chain were determined. Peptides derived from the oc-chain by tryptic digestion were isolated by paper ionophoresis and chromatography. The amino acid sequences were determined by the dansyl-Edman procedure or by further digestion with other enzymes.

scholarly journals The Fine Structure of the Sensory Epithelium of the Vomeronasal Organ in Suckling Rats

1971 ◽  
Vol 24 (3) ◽  
pp. 765 ◽  
Author(s):  
Jean E Kratzing
Keyword(s):  
Amino Acid ◽  
Gel Filtration ◽  
Vomeronasal Organ ◽  
Sensory Epithelium ◽  
Exchange Chromatography ◽  
Amino Acid Sequences ◽  
Tryptic Digestion ◽  
Tryptic Peptides ◽  
Special Procedure ◽  
A Chain

The amino acid sequence of the a-chain of haemoglobin from M. giganteus has been determined. The soluble peptides formed by tryptic digestion were isolated by gel filtration, ion-exchange chromatography, paper ionophoresis, and chromatography. The amino acid sequences were determined by the "dansyl"Edman procedure. Incomplete hydrolysis of one bond resulted in a large insolublecore peptide containing 40 amino acid residues. The sequence of this peptide was deduced from the sequences of smaller peptides resulting from further digestion with thermolysin and papain. Maleylation of the a-globin before tryptic digestion gave three large fragments which assisted in assigning tryptic peptides to specific areas of the molecule. A special procedure involving maleylation of a chymotryptic digest of globin was used to isolate peptides containing arginine which provided overlap sequences of tryptic peptides

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 Studies on Marsupial Protein. II. Amino Acid Sequence of the -Chain of Haemoglobin from the Grey Kangaroo, Macropus Giganteus

1969 ◽  
Vol 22 (6) ◽  
pp. 1437 ◽  
Author(s):  
GM Air ◽  
EOP Thompson
Keyword(s):  
Amino Acid ◽  
Ion Exchange ◽  
Amino Acid Sequence ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Amino Acid Sequences ◽  
Tryptic Digestion ◽  
Grey Kangaroo

The amino acid sequence of the jS-chain of haemoglobin from M. giganteus has been determined. The soluble peptides formed by tryptic digestion were isolated by gel filtration, ion-exchange chromatography, and paper ionophoresis, and amino acid sequences determined by the "dansyl"-Edman procedure. Special procedures were necessary for three peptides which were insoluble.

scholarly journals Haemoglobins of the Shark, Heterodontus Portusjacksoni II. Amino Acid Sequence of the a-Chain

1976 ◽  
Vol 29 (2) ◽  
pp. 73 ◽  
Author(s):  
AR Nash ◽  
WK Fisher ◽  
EOP Thompson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Paper Chromatography ◽  
Cyanogen Bromide ◽  
Gel Filtration ◽  
Amino Acid Sequences ◽  
Tryptic Digestion ◽  
Amino Terminal ◽  
Core Peptide ◽  
A Chain

The amino acid sequence of the a-chain of the principal haemoglobin from the shark, H. portusjacksoni has been determined. The chain has 148 residues and is acetylated at the amino terminal. The soluble peptides obtained by tryptic and chymotryptic digestion of the protein or its cyanogen bromide fragments were isolated by gel filtration, paper ionophoresis and paper chromatography. The amino acid sequences were determined by the dansyl-Edman procedure. The insoluble 'core' peptide from the tryptic digestion contained 34 residues and required cleavage by several proteases before the sequence was established. Compared with human a-chain there are 88 amino acid differences including the additional seven residues which appear on the amino terminal of the shark chain. There is also one deletion and one insertion. The chain contains no tryptophan but has four cysteinyl residues which is the highest number of such residues recorded for a vertebrate globin.

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.

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 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.

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