Amino-Acid Sequence of Sperm Whale Myoglobin

Nature ◽  
1965 ◽  
Vol 205 (4974) ◽  
pp. 883-887 ◽  
Author(s):  
ALLEN B. EDMUNDSON
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sperm Whale ◽  
Sperm Whale Myoglobin

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

Nature ◽  
1961 ◽  
Vol 190 (4777) ◽  
pp. 663-665 ◽  
Author(s):  
A. B. EDMUNDSON ◽  
C. H. W. HIRS
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sperm Whale ◽  
Chemical Studies ◽  
Sperm Whale Myoglobin

The amino acid sequence of human myoglobin and its minor fractions

1974 ◽  
Vol 186 (1084) ◽  
pp. 249-279 ◽  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Three Dimensional ◽  
Sperm Whale ◽  
Dimensional Structure ◽  
Human Haemoglobin ◽  
Human Myoglobin ◽  
Main Component ◽  
Haemoglobin Molecule ◽  
Sperm Whale Myoglobin

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.

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

1985 ◽  
Vol 38 (4) ◽  
pp. 347 ◽  
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.

The Croonian Lecture, 1968 - The haemoglobin molecule

1969 ◽  
Vol 173 (1031) ◽  
pp. 113-140 ◽  
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).

Differences in amino acid sequence between dolphin and sperm whale myoglobins

1970 ◽  
Vol 221 (1) ◽  
pp. 136-139 ◽  
Author(s):  
M. Karadjova ◽  
P. Nedkov ◽  
A. Bakardjieva ◽  
N. Genov
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sperm Whale

scholarly journals The antibody response to myoglobin is independent of the immunized species. Analysis in terms of replacements in the antigenic sites and in environmental residues of the cross-reactions of fifteen myoglobins with sperm-whale myoglobin antisera raised in different species

1980 ◽  
Vol 191 (3) ◽  
pp. 681-697 ◽  
Author(s):  
S S Twining ◽  
H Lehmann ◽  
M Z Atassi
Keyword(s):  
Amino Acid ◽  
Antibody Response ◽  
Three Dimensional ◽  
Sperm Whale ◽  
Cross Reactivity ◽  
Antigenic Structure ◽  
Amino Acid Substitutions ◽  
Antigenic Sites ◽  
The Cross ◽  
Sperm Whale Myoglobin

The recent determination of the entire antigenic structure of sperm-whale myoglobin with rabbit and goat antisera has permitted the examination of whether the antigenic structure recognized by antibodies depends on the species in which the antisera are raised. Also, by knowledge of the antigenic structure, the molecular factors that determine and influence antigenicity can be better understood in terms of the effects of amino acid substitutions occurring in the antigenic sites and in the environmental residues of the sites. In the present work, the myoglobins from finback whale, killer whale, horse, chimpanzee, sheep, goat, bovine, echidna, viscacha, rabbit, dog, cape fox, mouse and chicken were examined for their ability to cross-react with antisera to sperm-whale myoglobin. By immunoadsorbent titration studies with radioiodinated antibodies, each of these myoglobins was able to bind antibodies to sperm-whale myoglobin raised in goat, rabbit, chicken, cat, pig and outbred mouse. It was found that the extent of cross-reaction of a given myoglobin was not dependent on the species in which the antisera were raised. This indicated that the antibody response to sperm-whale myoglobin (i.e. its antigenic structure) is independent of the species in which the antisera are raised and is not directed to regions of sequence differences between the injected myoglobin and the myoglobin of the immunized host. Indeed, in each antiserum from a given species examined, that antiserum reacted with the myoglobin of that species. The extent of this auto-reactivity for a given myoglobin was comparable with the general extent of cross-reactivity shown by that myoglobin with antisera raised in other species. The cross-reactivities and auto-reactivities (both of which are of similar extents for a given myoglobin) can be reasonably rationalized in terms of the effects of amino acid substitutions within the antigenic sites and within the residues close to these sites. These findings confirm that the antigenicity of the sites is inherent in their three-dimensional locations.

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