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

Air, GM; Thompson, Eop

doi:10.1071/bi9691437

Cited by 27 publications

(7 citation statements)

References 7 publications

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“…The methods of enzyme digestion with trypsin, chymotrypsin, thermolysin and pepsin, of peptide mapping, of amino acid analysis and of sequence determination were substantially the same as described by Air and Thompson (1969) and Fisher and Thompson (1983).…”

Section: Peptide Isolation Amino Acid Analysis and Sequence Determinmentioning

confidence: 99%

Amino Acid Sequence of the ß-Chain of the Tetrameric Haemoglobin of the Bivalve Mollusc, Anadara trapezia

Gilbert¹,

Eo²

1985

Aust. Jnl. Of Bio. Sci.

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The amino acid sequence of the iJ-chain of the principal haemoglobin from A. trapezia has been determined. The sequence was deduced from the sequences of tryptic peptides, which were fractionated using highperformance liquid chromatography and peptide mapping. Additional sequence data, particularly for the large tryptic peptides, was obtained from enzyme digests of both cyanogen bromide fragments and large citraconyitryptic peptides.The iJ-chain has lSI residues which is longer than all the other sequenced haemoglobin chains except the a-chain of A. trapezia, which is 153 residues in length. The residues corresponding to those normally in the D helix are absent in this iJ-chain. The additional residues are contributed by an extension of the N-terminal region, which was also found to be acetylated.Comparison of the iJ-chain amino acid sequence with that of the a-chain of A. trapezia, the dimeric chain of A. trapezia, and the dimeric chain of A. broughtonii showed 53% identity in each case. In the E and F helices, the homology is particularly noticeable. There is 100% homology in the F helix of all four chains. The dimeric globin of A. trapezia also shows 100% homology with the iJ-chain in the E helix, while the a-chain shows 75 %.If the tertiary structure of the 0'-and iJ-chains of A. trapezia haemoglobin is the same as that of horse haemoglobin, then there are many changes in the aliJ2 contact site residues.

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Section: Peptide Isolation Amino Acid Analysis and Sequence Determinmentioning

confidence: 99%

Amino Acid Sequence of the ß-Chain of the Tetrameric Haemoglobin of the Bivalve Mollusc, Anadara trapezia

Gilbert¹,

Eo²

1985

Aust. Jnl. Of Bio. Sci.

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“…The methods of enzyme digestion with trypsin, chymotrypsin, pepsin, papain and staphylococcal protease; peptide mapping, amino acid analysis and sequence determination by the dansyl-Edman procedure were substantially the same as have been previously described Air and Thompson 1969;'Fisher and Thompson 1979;Webster and Thompson 1983). High performance liquid chromatography (HPLC) of peptide mixtures and identification of phenylthiohydantoin derivatives (PTH) were done as described by Webster and Thompson (1983).…”

Section: Peptide Isolation Amino Acid Analysis and Sequence Determinmentioning

confidence: 99%

Amino Acid Sequence Studies on Sheep Liver Fructose-bisphosphatase. II The Complete Sequence

Wk¹,

Eo²

1983

Aust. Jnl. Of Bio. Sci.

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The cyanogen bromide fragments of S-carboxymethylated fructose-bisphosphatase were purified. The amino acid sequences of the small fragments were determined by the dansyl-Edman method. The large fragments were subjected to proteolytic digestion to give smaller peptides more amenable for purification and sequencing by similar methods. Enzyme digests of the S-carboxymethylated enzyme gave overlap peptides containing the methionine residues.In conjunction with the amino acid sequence of the 60-residue N-terminal fragment previously determined on the S-peptide released by limited proteolysis with subtilisin the complete sequence of 336 residues was deduced. The sequence has been compared with the 335 residue sequence of pig kidney fructose-bisphosphatase and some areas of sequence for rabbit liver enzyme. The strong homology previously noted for the S-peptide sequences is maintained for the complete enzyme with only 34 changes in 336 residues when comparing the pig and sheep enzymes.

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“…18. S-Carboxymethyl-ADH samples were digested with trypsin (Worthington, N-tosylphenylalanine chloromethyl ketone-treated) according to ref.…”

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confidence: 99%

Structural analysis of an electrophoretically cryptic alcohol dehydrogenase variant from an Australian population of Drosophila melanogaster.

Chambers¹,

Laver²,

Campbell³

et al. 1981

Proc. Natl. Acad. Sci. U.S.A.

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

Cited by 27 publications

References 7 publications

Amino Acid Sequence of the ß-Chain of the Tetrameric Haemoglobin of the Bivalve Mollusc, Anadara trapezia

Amino Acid Sequence of the ß-Chain of the Tetrameric Haemoglobin of the Bivalve Mollusc, Anadara trapezia

Amino Acid Sequence Studies on Sheep Liver Fructose-bisphosphatase. II The Complete Sequence

Structural analysis of an electrophoretically cryptic alcohol dehydrogenase variant from an Australian population of Drosophila melanogaster.

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