scholarly journals Studies on Monotreme Proteins. III. Amino Acid Sequence of the a- and ß-Globin Chains of the Minor Haemoglobin from the Echidna, Tachyglossus Aculeatus Aculeatus

1973 ◽  
Vol 26 (6) ◽  
pp. 1327 ◽  
Author(s):  
EOP Thompson ◽  
WK Fisher ◽  
RG Whittaker
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Migration Rate ◽  
Minor Component ◽  
Amino Acid Sequences ◽  
Tryptic Digestion ◽  
Electrophoretic Migration ◽  
Globin Chains ◽  
Tachyglossus Aculeatus

Echidnas exhibit polymorphism in their haemoglobins. The minor component in animals from the mainland of Australia is Hb-IIA, which can be identified by electrophoretic migration rate and separated by chromatography on DEAE-Sephadex. This minor component has IX- and fi-globin chains which were only partially separated by chromatography on carboxymethylcellulose columns. By tryptic digestion of the partially purified chains, followed by fractionation by paper ionophoresis and chromatography, the component pep tides from the IX- and fi-chains were isolated and their amino acid sequences determined.

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 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 Studies on Monotreme Proteins II. Amino Acid Sequence of the a-Chain in Haemoglobin From the Echidna, Tachyglossus Aculeatus Aculeatus

1973 ◽  
Vol 26 (4) ◽  
pp. 877 ◽  
Author(s):  
RG Whittaker ◽  
WK Fisher ◽  
EOP Thompson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Paper Chromatography ◽  
Gel Filtration ◽  
Tryptic Digestion ◽  
A Chain ◽  
Tachyglossus Aculeatus

The amino acid sequence of the 141 residues of the IX-chain of the major haemoglobin (Hb-IB) from the echidna has been determined. The soluble peptides formed by tryptic digestion were isolated by gel filtration, paper ionophoresis, and paper chromatography.

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 Studies on the high-sulphur proteins of reduced Merino wool. Amino acid sequence of protein SCMKB-IIIA3

1973 ◽  
Vol 133 (4) ◽  
pp. 641-654 ◽  
Author(s):  
Louis S. Swart ◽  
Thomas Haylett
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Minor Component ◽  
Amino Acid Sequences ◽  
Edman Degradation ◽  
Merino Wool ◽  
C Terminus ◽  
A Minor

The complete amino acid sequences of wool protein SCMKB-IIIA3 (131 residues) and a minor component SCMKB-IIIA3A (130 residues) have been determined. The proteins are mutually homologous and have free threonine as the N-terminal residue and carboxymethylcysteine as the C-terminus. The peptides used for the sequence work were obtained by trypsin, thermolysin, pepsin and chymotrypsin digestions and were fractionated by chromatography on DEAE-cellulose, gel filtration on Sephadex G-25 and G-50, paper chromatography and electrophoresis. The Edman degradation method (employing both the Beckman Sequencer and a non-automatic procedure) was used to obtain the sequences of the peptides.

Carnivora: The Primary Structure of the Major and Minor Hemoglobin Components of Adult North Persian Leopard (Panthera pardus sexicolor)

1988 ◽  
Vol 43 (10) ◽  
pp. 1341-1346 ◽  
Author(s):  
Aftab Ahmed ◽  
Meeno Jahan ◽  
Gerhard Braunitzer ◽  
Reinhard Göltenboth
Keyword(s):  
Amino Acid ◽  
Gas Phase ◽  
Primary Structure ◽  
Minor Component ◽  
Reversed Phase ◽  
Amino Acid Sequences ◽  
Globin Chains ◽  
Total Hemoglobin ◽  
Persian Leopard ◽  
Polypeptide Chains

The complete primary structure of the two hemoglobin components of the adult North Persian Leopard are presented. The major component Hb-I accounts for 80-90% and the minor component Hb-II accounts for 20-10% of the total hemoglobin. Reversed phase HPLC was used for the separation of the polypeptide chains. The amino acid sequences were established by automated Edman degradation of the globin chains and of the tryptic peptides in liquid-and gas-phase sequenators. The sequences are aligned with those of human Hb-A. Our result shows that the hemoglobins of North Persian Leopard and Jaguar are identical in amino acid sequence.

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 VII. Amino Acid Sequence of Myoglobin From the Platypus, Ornithorhynchus Anatinus

1976 ◽  
Vol 29 (2) ◽  
pp. 57 ◽  
Author(s):  
WK Fisher ◽  
EOP Thompson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Amino Acid Sequences ◽  
Amino Acid Residues ◽  
Similar Treatment ◽  
Globin Chains ◽  
Ornithorhynchus Anatinus ◽  
Constant Rate ◽  
Human Myoglobin

Myoglobin isolated from skeletal. muscle of the platypus contains 153 amino acid residues. lhe complete amino acid sequence has been determined following cleavage with cyanogen bromide and further digestion of the four fragments with trypsin, chymotrypsin, pepsin and thermolysin. Sequences of the purified peptides were determined by the dansyl-Edman procedure. The amino acid sequence showed 25 differences from human myoglobin and 24 from kangaroo myoglobin. Amino acid sequences in myoglobins are more conserved than sequences in the exand fi-globin chains, and platypus myoglobin shows a similar number of variations in sequence to kangaroo myoglobin when compared with myoglobin of other species. The date of divergence of the platypus from other mammals was estimated at 102 � 31 million years, based on the number of amino acid differences between species and allowing for multiple mutations during the evolutionary period. This estimate differs widely from the estimate given by similar treatment of the ex- and fi-chain sequences and a constant rate of mutation .of globin chains is not supported.

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