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PubMed1998

The role of distal histidine in peroxidase activity of myoglobin--transient-kinetics study of the reaction of H2O2 with wild-type and distal-histidine-mutanted recombinant human myoglobin.

The distal histidine has been proposed to play a crucial role in the reaction of peroxidases with hydroperoxide. Myoglobin (Mb), due to its close similarity with peroxidases, also reacts with various peroxides. The effect of mutation of the distal histidine on the peroxidase activity of Mb has been investigated by stopped-flow kinetics of the reaction of hydrogen peroxide with wild-type Mb and [Gly64]Mb. The results indicate kinetic and mechanistic differences in the formation of peroxide compounds from these two forms of Mb. The rate of reaction of H2O2 with the wild-type Mb decreased 8-9-fold on mutation of the distal histidine to glycine ([Gly64]Mb). A second slow phase was observed for the reaction of H2O2 with [Gly64]Mb, but was not observed in the corresponding reaction with wild-type Mb. It is suggested that the decrease in the rate of the reaction on mutation is due to the absence of a general acid-base catalyst. The effect of pH on the rate of reaction of H2O2 with wild-type Mb and [Gly64]Mb is contrasting. While the rate of the Mb [corrected] reaction decreased for wild-type Mb at higher pH, probably due to the acid-alkaline transition of Mb at higher pH, the rate of reaction was found to increase at higher pH for mutant Mb. The increase in the rate of the reaction is suggested to be due to an increase in the ionization of H2O2 at higher pH, the rate-determining step being the formation of the intermediate Fe-O-O-H complex and not the subsequent step of oxo-ferryl complex formation. The thermodynamic parameters calculated from the temperature-dependent study showed that the enthalpy of binding of H2O2 with Mb is positive, indicating that the process is endothermic. The apparent energy of activation of the reaction of H2O2 with Mb was found to be higher than that of peroxidases, suggesting that this may be oue of the reasons for the slower rate of the reaction of H2O2 with Mb compared with peroxidases.

Amino Acid Sequence↗
PubMed1985

Shark myoglobins. II. Isolation, characterization and amino acid sequence of myoglobin from Galeorhinus japonicus.

Native oxymyoglobin (MbO2) 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 MbO2. However, the pH-dependence for the autoxidation of MbO2 was seen to be quite different from that of sperm whale (Physeter catodon) MbO2. 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.

Amino Acid Sequence↗
PubMed1981

T cell clones reactive with sperm whale myoglobin. Isolation of clones with specificity for individual determinants on myoglobin.

We have been able to isolate clones of sperm whale muscle myoglobin (Mb)-reactive T cells from (C57BL/6 x A/J)F1 [(B6A)F1] mice. Four types of clones were isolated, distinguished by their patterns of recognition of Mb cyanogen bromide (CNBr) fragments and antigen presenting cell (APC) requirements. Individual T cell clones proliferated in response to one of three CNBr fragments of Mb. Dose-response curves of all clones were identical for native Mb and the appropriate fragment. T cell clones reactive to fragment 1-55 did not proliferate in response to peptide 15-22 (a peptide that binds to serum antibody directed against 1-55). These data support previous findings suggesting differences between antigen recognition by T and B cells, i.e., T cells may not recognize antigen in its native conformation and/or T and B cells may recognize distinct epitopes on the same antigen. Using T cell clones to analyze genetic control of responsiveness to Mb, we found that certain (B6A)F1 T cells recognize Mb presented by low responder strain APC. Thus, genetically determined low responsiveness in this case is probably not due to failure of APC function. We also found that responsiveness to certain Mb epitopes mapped to the I-A subregion whereas others mapped, via gene complementation, to the I-A and I-E subregions. We found no examples of responsiveness mapping to the I-C subregion and suggest an alternative explanation for previous reports mapping genetic control of responsiveness to certain Mb determinants to I-C.

Animals↗
PubMed1986

The mouse myoglobin gene. Characterisation and sequence comparison with other mammalian myoglobin genes.

Seal myoglobin (Mb) exons 1 and 3 were used as probes to isolate the functional mouse Mb gene. This gene has a very low level of Mb expression in skeletal muscle. Although it is shorter, the mouse Mb gene displays the common organisation found in human and seal Mb genes. In addition, we have defined blocks of conserved sequences in the 5' flanking region by comparison with other mammalian Mb genes. Moreover, about 10(3) bases upstream of the cap site we identified a repetitive B1 element directly associated with two overlapping open reading frames, containing a putative polyadenylation signal. A polypyrimidine-rich region has also been located upstream from the gene.

Animals↗
PubMed1991

NMR study of Galeorhinus japonicus myoglobin. 1H-NMR evidence for a structural alteration on the active site of G. japonicus myoglobin upon azide ion binding.

The heme molecular structure of the met-azido form of the myoglobin from the shark Galeorhinus japonicus has been investigated by 1H NMR. A nuclear Overhauser effect (NOE) was clearly observed among the heme peripheral side-chain proton signals of this complex, which undergoes thermal spin equilibrium between high-spin (S = 5/2) and low-spin (S = 1/2) states, and the NOE connectivities provided the assignment of the resonances from the heme C13(1)H2 and C17(1)H2 protons. Chemical shift inequivalence of these proton resonances not only provided information about the orientation of these methylene protons with respect to the heme plane, but also allowed characterization of the time-dependent build-up of the NOE between them, which yields the correlation time for the internal motion of the inter-proton vector. The relatively large mobility found for the C17(1)H2 group suggests that the carboxyl oxygen of the heme C17 propionate is not anchored to the apo-protein by a salt bridge. It has been shown that the ferric high-spin form of G. japonicus Mb possesses a penta-coordinated heme [Suzuki, T. (1987) Biochim. Biophys. Acta 914, 170-176; Yamamoto, Y., Osawa, A., Inoue, Y., Chûjô, R. & Suzuki, T. (1990) Eur. J. Biochem. 192, 225-229] and that the conformation of both heme propionate groups is fixed with respect to the heme, as well as the apo-protein, by a salt bridge [Yamamoto, Y., Inoue, Y., Chûjô, R. & Suzuki, T. (1990) Eur. J. Biochem. 189, 567-573]. Therefore the weakening or interruption of the interaction between the C17 propionate and His FG3 upon the changes of the coordination and spin state of the heme iron, during azide ion binding to ferric high-spin G. japonicus Mb, is attributed to the displacement of the FG corner of the apoprotein away from the heme C17 propionate group. A similar structural alteration has been revealed by X-ray structural analyses of unliganded and liganded forms of ferrous hemoproteins [Baldwin, J. & Chothia, C. (1979) J. Mol. Biol. 129, 175-220; Phillips, S.E.V. (1980) J. Mol. Biol. 142, 531-554].

Animals↗
PubMed1983

T-lymphocyte recognition of sperm-whale myoglobin. Recognition of synthetic peptides carrying antigenic site 5 by myoglobin-primed T-cells.

Previous studies from this laboratory have resulted in the determination of the antigenic structure of sperm-whale myoglobin (Mb). In the present work, we have investigated the fine specificity requirements for T-cell recognition of one of the Mb antigenic sites (antigenic site 5). The antigenic site (peptide 145-153) and seven progressively longer peptides, increasing in length stepwise by two residues at a time, up to 22 residues in length (peptide 132-153), were synthesized. In addition, four truncated peptides were synthesized with intentional deletions at Tyr-151 and Ala-144. The T-cell recognition of these purified synthetic peptides was examined here in detail in three strains of mice (BALB/cByJ, B10.D2/n and SJL/J). Mb-primed mice afforded T-cells which proliferated to smaller peptides (two or four residues longer than the site; i.e. peptides 145-153 and 143-153) and more so to the longer peptides 135-153 and 132-153 and to Mb. No response was obtained to the truncated peptides, thus underscoring the fine specificity T-cells. No response was obtained also to intermediate-sized peptides. The latter result, due to an unfavourable mode of folding, suggested a conformational dependency in T-lymphocyte recognition.

Animals↗
PubMed1983

T-lymphocyte recognition of sperm-whale myoglobin. Specificity of T-cell recognition following neonatal tolerance with either myoglobin or synthetic peptides of an antigenic site.

Recently, in investigating the responses of T-cells from high responder mice that were primed with myoglobin (Mb) or with synthetic peptides containing antigenic site 5 and increasing in length stepwise by increments of two residues, we observed that T-cell recognition was highly dependent on conformation. In the present studies, tolerization experiments were carried out to further investigate this finding. Neonatal mice (BALB/cByJ) were either tolerized with Mb or with synthetic peptides of Mb containing antigenic site 5. Tolerization with Mb and subsequent immunization with Mb gave T-cells that did not proliferate in vitro to Mb or any of the peptides. T-cells from mice that were tolerized with a truncated peptide 139-153 (having deletions at Tyr-151 and Ala-144) and subsequently immunized with Mb proliferated in vitro to Mb and to peptides 132-153, 135-153 and 143-153. T-cells from mice that were tolerized with native Mb and subsequently immunized with peptides (which are unfolded in solution) did not proliferate in vitro to Mb, but responded well to the peptides. Conversely, tolerization with peptides had no effect on the recognition of, and the response to, native Mb by the T-cells, whereas the response to the peptides was completely removed. It was thus concluded that the recognition of protein antigens (or at least of Mb) by T-cells is (like the recognition by antibody) dependent on the conformation of the antigen.

Animals↗
PubMed1984

Depressed in vitro and in vivo antibody response and adoptive transfer of delayed hypersensitivity to myoglobin with spleen cells of mice chronically infected with Schistosoma japonicum and injected with myoglobin.

Spleen cells from C57BL/6J mice infected for 21 weeks with Schistosoma japonicum did not show an in vitro secondary antibody response upon challenge with sperm whale myoglobin. Mice infected for 13 weeks showed almost no in vivo secondary antibody response to this antigen. Spleen cells from mice infected for 12 to 21 weeks did not adoptively transfer delayed hypersensitivity to this antigen.

Animals↗
PubMed2000

Concentrations of myoglobin and myoglobin mRNA in heart ventricles from Antarctic fishes.

We used a combined immunochemical and molecular approach to ascertain the presence and concentrations of both the intracellular oxygen-binding hemoprotein myoglobin (Mb) and its messenger RNA (mRNA) in 13 of 15 known species of Antarctic channichthyid icefishes. Mb protein is present in the hearts of eight species of icefishes: Chionodraco rastrospinosus, Chionodraco hamatus, Chionodraco myersi, Chaenodraco wilsoni, Pseudochaenichthys georgianus, Cryodraco antarcticus, Chionobathyscus dewitti and Neopagetopsis ionah. Five icefish species lack detectable Mb protein: Chaenocephalus aceratus, Pagetopsis macropterus, Pagetopsis maculatus, Champsocephalus gunnari and Dacodraco hunteri. Mb concentrations range from 0.44+/-0.02 to 0.71+/-0.08 mg Mb g(-)(1 )wet mass in heart ventricle of species expressing the protein. A Mb-mRNA-specific cDNA probe was used to quantify mRNA in five Mb-expressing icefishes. Mb mRNA was found in low but detectable amounts in Champsocephalus gunnari, one of the species lacking detectable Mb. Mb mRNA concentrations in heart ventricle from Mb-expressing species ranged from 0.78+/-0.02 to 16.22+/-2.17 pg Mb mRNA microg(-)(1 )total RNA). Mb protein and Mb mRNA are absent from the oxidative skeletal muscle of all icefishes. Steady-state concentrations of Mb protein do not parallel steady-state concentrations of Mb mRNA within and among icefishes, indicating that the concentration of Mb protein is not determined by the size of its mRNA pool.

Animals↗
PubMed1988

Determination of serum level of myoglobin and plasma level of autoantibodies to myoglobin in patients with angina pectoris.

The serum level of myoglobin (Mb) was determined in 11 male patients with chronic ischemic heart disease (angiographically studied) by the mean of an enzyme immunoassay (EIA). By a second EIA we could detect in all our patients autoantibodies (autoAB) to Mb. While the level of Mb in all cases was normal (less than 100 ng/ml) we found differences in the level of autoAB to Mb (normal value 90-100%). 7 patients with unstable Angina pectoris exhibited decreased levels of autoAB to Mb (65%). In 4 patients with stable Angina pectoris autoAB to Mb were 93%. The physiological role of the autoAB to Mb remains still unclear. The simultaneous determination of Mb and the autoAB to Mb may be helpful in differential diagnosis of stable and unstable Angina pectoris.

Adult↗
PubMed1979

[A study on the physiological basis of training effect--with special reference to myoglobin. I. Isolation and properties of myoglobin from dog skeletal muscle (author's transl)].

Myoglobin (Mb) was isolated from canine skeletal muscle by a novel heat denaturation-gel filtration-ion exchange chromatography procedure. The purified major Mb was homogeneous by gel electrophoretic and ultracentrifugal analysis, and the sedimentation coefficient at infinite dilution (S degrees 20, w) was 1.9 S. The molecular weight by sedimentation equilibrium was 1.72 X 10(4) and was essentially identical with the values by the iron analysis (1.80 X 10(4) and the amino acid composition (1.78 X 10(4). The spectroscopic properties of deoxy-, oxy-, carbonmonoxy- and met-derivatives of the Mb were determined in ultraviolet, Soret and visible regions. The pK' of acid-alkaline transition of the met-Mb was estimated as 8.80+/-0.04 (25 degrees) from the pH-dependent spectral change. The oxygen equilibrium studies revealed complete absence of such allosteric properties as heme-heme interaction, anion effect and the Bohr effect which were always present in normal mammalian hemoglobins. Oxygen tension for the half-oxygenation was 0.48 mmHg (20 degrees) and its temperature-dependent change gave the delta H degrees of -15.7 Kcal/mole.

Amino Acids↗
PubMed1979

Preparation of ruthenium(II) and ruthenium(III) myoglobin and the reaction of dioxygen, and carbon monoxide, with ruthenium(II) myoglobin.

Ruthenium myoglobins have been prepared by the reconstitution of horse heart apomyoglobin with either ruthenium(II) or ruthenium(III) mesoporphyrin IX (MpIX) derivatives. The ruthenium(II) and -(III) myo globins (RuMb and RuMb+, respectively) contain one ruthenium porphyrin/heme binding site; the species are readily interconverted using dithionite for reduction and bromine for oxidation. RuMb binds carbon monoxide to give the known carbonyl complex. Reversible oxygenation occurs readily with protein-free RuII(MpIX) species in dimethylformamide, but RuMb in phosphate buffer is irreversibly oxidized by dioxygen to give RuMb+ via an outer sphere electron transfer mechanism.

Animals↗