The Amino-Acid Sequence of Sperm Whale Myoglobin: Chemical Studies

The complete amino acid sequence of human skeletal myoglobin is described. That of heart myoglobin is found by homology to be the same. When myoglobin is prepared some minor fractions may be obtained besides the main component. They are shown to be artefacts arising from deamidations. The likely three-dimensional structure of human myoglobin is discussed, taking that of sperm-whale myoglobin as a reference. Human myoglobin is compared with the α - and β -chains of human haemoglobin. There is a noteworthy similarity of internal residues and haem contacts, but little resemblance of sites where the haemoglobin chains form dimeric and tetrameric contacts, when they become subunits of the haemoglobin molecule.

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Shark Myoglobins. II.Isolation, Characterization and Amino Acid Sequence of Myoglobin from Galeorhinus japonicus

Australian Journal of Biological Sciences ◽

10.1071/bi9850347 ◽

1985 ◽

Vol 38 (4) ◽

pp. 347 ◽

Cited By ~ 19

Author(s):

Tomohiko Suzuki ◽

Takanobu Suzuki ◽

Tohru Yata

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Sequence Homology ◽

Chromatographic Separation ◽

Ph Dependence ◽

Deae Cellulose ◽

Sperm Whale ◽

Amino Terminus ◽

Red Muscle

Native oxymyoglobin (Mb02) was isolated from red muscle of G. japonicus by chromatographic separation from metmyoglobin (metMb) on DEAE-cellulose and the amino acid sequence of the major chain was determined with the aid of sequence homology with that of G. australis. It was shown to differ in amino acid sequence from that of G. australis by 10 replacements, to be acetylated at the amino terminus and to contain glutamine at the distal (E7) residue. It was also shown to have a spectrum very similar to that of mammalian Mb02. However, the pH-dependence for the autoxidation of Mb02 was seen to be quite different from that of sperm whale (Physeter catodon) Mb02. Although the sequence homology between sperm whale and G. japonicus myoglobins is about 40%, their hydropathy profiles were very similar, indicating that they have a similar geometry in their globin folding.

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Coordination complexes and catalytic properties of proteins and related substances. 79. The complete amino acid sequence of the major component myoglobin of dwarf sperm whale (Kogia simus)

Biochemistry ◽

10.1021/bi00624a010 ◽

1977 ◽

Vol 16 (5) ◽

pp. 873-877 ◽

Cited By ~ 21

Author(s):

Francis E. Dwulet ◽

Barry N. Jones ◽

Lee D. Lehman ◽

Frank R. N. Gurd

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Catalytic Properties ◽

Sperm Whale ◽

Coordination Complexes ◽

Complete Amino Acid Sequence ◽

Related Substances

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Assignment of heme and distal amino acid resonances in the 1H-NMR spectra of the carbon monoxide and oxygen complexes of sperm whale myoglobin

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology ◽

10.1016/0167-4838(85)90329-2 ◽

1985 ◽

Vol 832 (2) ◽

pp. 175-185 ◽

Cited By ~ 49

Author(s):

Bridget C. Mabbutt ◽

Peter E. Wright

Keyword(s):

Carbon Monoxide ◽

Amino Acid ◽

1H Nmr ◽

Nmr Spectra ◽

Sperm Whale ◽

1H Nmr Spectra ◽

Sperm Whale Myoglobin ◽

Oxygen Complexes

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Evidence for the amino acid sequence of porcine pancreatic elastase

Biochemical Journal ◽

10.1042/bj1310643 ◽

1973 ◽

Vol 131 (4) ◽

pp. 643-675 ◽

Cited By ~ 37

Author(s):

David M. Shotton ◽

Brian S. Hartley

Keyword(s):

Molecular Weight ◽

Amino Acid ◽

Amino Acid Sequence ◽

Polypeptide Chain ◽

Pancreatic Elastase ◽

Single Polypeptide Chain ◽

Chemical Studies ◽

Lending Library ◽

Porcine Pancreatic Elastase ◽

Single Polypeptide

The preparation and purification of tryptic peptides from aminoethylated Dip-elastase and [14C]carboxymethylated Dip-elastase, and of peptic peptides from native elastase is described. A summary of the results of chemical studies used to elucidate the amino acid sequence of these peptides is presented. Full details are given in a supplementary paper that has been deposited as Supplementary Publication SUP 50016 at the National Lending Library for Science and Technology, Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1973), 131, 1–20. These results, together with those from previously published papers, are used to establish the complete amino acid sequence of elastase, which is a single polypeptide chain of 240 residues, molecular weight 25900, containing four disulphide bridges.

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Nucleotide sequence analysis of the gene encoding the Deinococcus radiodurans surface protein, derived amino acid sequence, and complementary protein chemical studies.

Journal of Bacteriology ◽

10.1128/jb.169.11.5216-5223.1987 ◽

1987 ◽

Vol 169 (11) ◽

pp. 5216-5223 ◽

Cited By ~ 58

Author(s):

J Peters ◽

M Peters ◽

F Lottspeich ◽

W Schäfer ◽

W Baumeister

Keyword(s):

Amino Acid ◽

Sequence Analysis ◽

Nucleotide Sequence ◽

Amino Acid Sequence ◽

Deinococcus Radiodurans ◽

Surface Protein ◽

Nucleotide Sequence Analysis ◽

Gene Encoding ◽

Chemical Studies

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Chemical studies on the cyanogen bromide peptides of rat skin collagen. Amino acid sequence of α1-CB4

Biochemistry ◽

10.1021/bi00787a018 ◽

1971 ◽

Vol 10 (11) ◽

pp. 2076-2081 ◽

Cited By ~ 57

Author(s):

William Thomas Butler ◽

Sharon L. Ponds

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Cyanogen Bromide ◽

Rat Skin ◽

Skin Collagen ◽

Chemical Studies

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The Croonian Lecture, 1968 - The haemoglobin molecule

Proceedings of the Royal Society of London Series B Biological Sciences ◽

10.1098/rspb.1969.0043 ◽

1969 ◽

Vol 173 (1031) ◽

pp. 113-140 ◽

Cited By ~ 129

Keyword(s):

Amino Acid ◽

Oxygen Carrier ◽

Sperm Whale ◽

Amino Acid Sequences ◽

Single Chain ◽

X Ray ◽

Isomorphous Replacement ◽

Twofold Symmetry Axis ◽

The Right ◽

Sperm Whale Myoglobin

Haemoglobin is the respiratory protein of the red blood cells which carries oxygen from the lungs to the tissues and facilitates, both directly and indirectly, the return transport of carbon dioxide. Mammalian haemoglobin has a molecular weight of 64500 and contains two pairs of polypeptide chains: the α -chains with 141 amino acid residues each and the β -chains with 146. Each chain is combined with one haem. Myoglobin, the oxygen carrier of muscle, is closely related to haemoglobin, but has a simpler constitution: it consists of only one polypeptide chain of 153 residues and a single haem. The amino acid sequences of the myoglobins and haemoglobins of man and of several animals have been determined (Dayhoff & Eck 1968). By means of the method of isomorphous replacement with heavy atoms, X-ray analysis of sperm whale myoglobin at 2·0 Å resolution provided the first solution of the structure of a protein (Kendrew et al . 1960; Watson 1969). All but 21 of its 153 residues form part of helices; over most of their length these helices have conformations closely resembling the right-handed α -helix of Pauling & Corey (1951). The chain is divided into 8 helical segments, separated by corners or non-helical regions. Together these form a kind of basket into which the haem group fits neatly, so that only its propionic acid side-chains protrude into the surrounding liquid (figures 1, 2). X-ray analysis at 5·5 Å resolution showed each chain of horse haemoglobin to be folded in much the same way as the single chain of sperm whale myoglobin. The 4 chains are arranged tetrahedrally, each carrying one haem in a pocket near the protein surface. The chemically identical halves of the molecule are related by a twofold symmetry axis (figure 3, plate 18; Cullis et al . 1962).

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