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PubMed1980

Properties of monoclonal antibodies specific for determinants of a protein antigen, myoglobin.

Monoclonal hybridoma antibodies specific for the protein antigen sperm whale myoglobin were produced using hyperimmune spleen cells from mice with the genetic trait of high responsiveness to myoglobin. Antibodies from the several clones tested were found to produce linear Scatchard plots, as predicted for homogeneous antibodies, and to possess high affinities for the immunogen (KA congruent to 10(9) M-1). None of the monoclonal antibodies tested reacted with either fragment (1-55) or fragment (132-153) of sperm whale myoglobin. Competitive binding assays using human and horse myoglobins suggested that several of these monoclonal antibodies, which can readily distinguish these myoglobins, recognize different antigenic determinants on the myoglobin molecule. Studies using additional myoglobin sequence variants as competitors should be able to more closely define these antigenic determinants.

Animals↗
PubMed1983

Reactivity of ferrous heme proteins at low pH.

The pH rate profile of sperm whale myoglobin (Mb) reacting with CO has been confirmed to follow the behavior previously reported (Giacometti, G.M., Traylor, T.G., Ascenzi, P., Brunori, M., and Antonini, E. (1977) J. Biol. Chem. 252, 7447-7448), and appears to be different from that obtained by others. The pH investigation has been extended to the CO-binding rates of Chironomus thummi thummi erythrocruorin and Aplysia limacina Mb, whose pH rate profile is different from that of sperm whale Mb. Besides the "base dissociation" mechanism previously invoked, the iron atom-heme plane distance is discussed as a possible determinant of the CO reactivity in these monomeric heme proteins.

Animals↗
PubMedDate not supplied

[Comparative study of the RNA and proteins of antigenically similar human and animal influenza A viruses].

In 1976-1979 in various regions of the USSR influenza viruses were isolated from mammals and birds and found to be antigenically similar with human influenza viruses having hemagglutinin H0, H1, and neuraminidase N1. Comparative studies of electrophoretic mobility in polyacrylamide gel of RNAs and proteins of these viruses and human influenza viruses sharing common antigens with them were carried out. By the mobility in gel of genome fragments, the virus isolated from a squirrel, A/squirrel/Vladivostok/1004/79 (H0N1), was found to be similar to human A/PR/8/34 (H0N1) virus; both viruses had a similar polypeptide composition. In contrast, the virus isolated in 1978 from a turkey, A/turkey/Kiev/292/78 (H1N1), by the mobility in gel of genome fragments including those coding for hemagglutinin and neuraminidase differed significantly from antigenically similar epidemic viruses: A/FM/1/47/ (H1N1) and a virus isolated during an epidemic in the same year, A/USSR/90/77/ (H1N1) despite the similarity with the latter in the polypeptide spectrum. Hemagglutinin of a virus isolated in 1976 from blue whales, A/whale/TO/19/76, was serologically identified as HO, neuraminidase of this virus as Nav2. An analysis of genome fragments of the whale virus showed the gene 4 coding for hemagglutinin to be similar by mobility in gel with the corresponding fragment of human influenza virus A/PR/8/34 (H0N1), and the gene 6 coling for neuraminidase in most influenza A viruses to be similar by mobility in gel with the gene 6 of A/pintail/Primorie/695/76 (H2Nav2) virus. An analysis of proteins of this virus by mobility in gel showed all its proteins, with the exception of one with a molecular weight of about 70,000 daltons, to be similar with those of human A/PR/8/34 (H0N1) virus. The protein with the molecular weight of about 70,000 daltons is assumed to be neuraminidase of the second avian type (Nav2). A similar protein was found in avian viruses A/pintail/Primorie/18/76 (H2Nav2), and A/tern/Turkmenia/18/73 (Hav7 Nav2). The antigenic analysis of these strains using a panel of 6 monoclonal antibody to the A/Brazil/11/76 (H1N1) strain revealed a close similarity in the antigenic structure of hemagglutinin of human influenza virus A/USSR/90/77 (H1N1) which had caused an epidemic outbreak in the USSR in 1977-1978 and A/turkey/Kiev/292/78 (H1N1) virus. Human and animal influenza viruses with hemagglutinin of the HO type did not react with any of the 6 clones under study.

Animals↗
PubMed1994

Memorial stones for the souls of animals killed for human welfare in Japan.

In Japan, at the old ports of the whaling industry, at all 365 slaughterhouses of the country, at some of the more than 90 wholesale markets of marine products, and at most of the about 170 testing facilities using laboratory animals, there are memorial stones for the souls of the animals killed for human welfare. Except at the whaling ports, where the memorials often can be dated back to the 17. century, all stones have been erected in the 20. century, most of them during the last 2 decades. The roots of this Japanese folk custom are probably in the prehistoric times of Shintoism. With the introduction of Buddhism in the 6. century, the killing of animals was considered sinful. Following the opening of the country in 1860, slaughterhouses were established.

Abattoirs↗
PubMed1993

Ligand diffusion in the distal heme pocket of myoglobin. A primary determinant of geminate rebinding.

There are at least two picosecond kinetic components in the rebinding of NO to native sperm whale myoglobin. Petrich et al. (Petrich, J. W., Lambry, J.-C., Kuczera, K., Karplus, M., Poyart, C., and Martin, J.-L. (1991) Biochemistry 30, 3975-3987) attribute the slowing of the reaction to a movement of the iron atom out of the plane of the heme following ligand dissociation. In contrast, Gibson et al. (Gibson, Q. H., Regan, R., Elber, R., Olson, J. S., and Carver, T. E. (1992) J. Biol. Chem. 267, 22022-22034) have explained multiphasic geminate reactions by diffusion of NO into the distal heme pocket as determined by its detailed structure. O2 and NO rebinding to iron and cobalt derivatives of native, V68F, and V68I sperm whale myoglobin has been examined. Each iron protein shows a biphasic time course of NO rebinding reactions with widely different rates and amplitudes. Although cobalt does not move out of the plane of the porphyrin on ligand removal, the reactions of the iron and cobalt derivatives of each protein were closely similar. The time course of O2 rebinding to cobalt was also similar to that of NO rebinding to iron. These results are consistent with a primary role for the structure of the distal pocket in determining diffusion of ligands away from the metal atom and as a result the time course of picosecond ligand rebinding.

Animals↗
PubMed1993

The mechanism of autooxidation of myoglobin.

Time courses for the autooxidation of native and mutant sperm whale and pig myoglobins were measured at 37 degrees C in the presence of catalase and superoxide dismutase. In sperm whale myoglobin, His64(E7) was replaced with Gln, Gly, Ala, Val, Thr, Leu, and Phe; Val68(E11) was replaced with Ala, Ile, Leu, and Phe; Leu29(B10) was replaced with Ala, Val, and Phe. In pig myoglobin, His64(E7) was replaced with Val; Val68(E11) was replaced with Thr and Ser; Thr67(E10) was replaced with Ala, Val, Glu, and Arg; Lys45(CD3) was replaced with Ser, Glu, His, and Arg. The observed pseudo-first order rate constants varied over 4 orders of magnitude, from 58 h-1 (H64A) to 0.055 h-1 (native) to 0.005 h-1 (L29F) at 37 degrees C, pH 7, in air. The dependences of the observed autooxidation rate constant on oxygen concentration and pH were measured for native and selected mutant myoglobins. In the native proteins and in most mutants still possessing the distal histidine, autooxidation occurs through a combination of two mechanisms. At high [O2], direct dissociation of the neutral superoxide radical (HO2) from oxymyoglobin dominates, and this process is accelerated by decreasing pH. At low [O2], autooxidation occurs by a bimolecular reaction between molecular oxygen and deoxymyoglobin containing a weakly coordinated water molecule. The neutral side chain of the distal histidine (His64) inhibits autooxidation by hydrogen bonding to bound oxygen, preventing both HO2 dissociation and the oxidative bimolecular reaction with deoxymyoglobin. Replacement of His64 by amino acids incapable of hydrogen bonding to the bound ligand markedly increases the rate of autooxidation and causes the superoxide mechanism to predominate. Increasing the polarity of the distal pocket by substitution of Val68 with Ser and Thr accelerates autooxidation, presumably by facilitating protonation of the Fe(II).O2 complex. Increasing the net anionic charge at the protein surface in the vicinity of the heme group also enhances the rate of autooxidation. Decreasing the volume of the distal pocket by replacing small amino acids with larger aliphatic or aromatic residues at positions 68 (E11) and 29 (B10) inhibits autooxidation markedly by decreasing the accessibility of the iron atom to solvent water molecules.

Animals↗
PubMedDate not supplied

[Characteristics of the process of oxidation of fats of diverse character during storage].

The process of various commercial fats, such as cod oil, edible whale and sperm oil, as well as sunflower seed oil oxidation occurring under the effect of atmospheric oxygen was investigated. The susceptibility of fats to oxidation was found to be determined by the degree of their unsaturation, conditioned by the composition of fatty acids. During oxidation of cod and edible whale oil under test conditions there takes place decomposition of biologically active acids with 5 and 6 double bonds, which is most strongly pronounced in unsaturated cod oil and thus bears witness to a materially diminished nutritional value of these oils. The data obtained proves the advisability of storing different fats under dissimilar conditions and confirm the need for using highly effective means for inhibiting the processes of the cod oil oxidation, this oil being used for medical purposes.

Animals↗
PubMed1997

[Problems of disposal of dead marine mammals].

Feasibilities and limits to dispose stranded large whales and the risk of the staff during the salvage and dissection of these animals are described here. The influence on the environment by leaving large marine mammals in the place of stranding are exemplary discussed in connection with the accumulation of toxins of Clostridium botulinum in the food chain as a source of danger for water fowls of the coastal region. Therefore carcasses of whales must be removed from the shore after their stranding. Under special circumstances the carcasses could be lowered into a dune.

Animals↗
PubMed1988

T cell response to myoglobin: a comparison of T cell clones in high-responder and low-responder mice.

Mice carrying the H-2b haplotype (e.g., inbred strains C57BL/6 and C57BL/10) are low responders to sperm whale myoglobin when tested in the T cell proliferation assay. Their response is improved by the removal of the Ly-2+ cells from the lymph node population, but it still remains significantly lower than that of cells cells from high-responder strains (e.g., DBA/2, H-2d). To determine whether T cells from the low and high-responder mice recognize the same or different epitopes on the immunizing antigen, we obtained sets of T cell clones from both strains and tested them against peptides representing different regions of the myoglobin molecule, as well as against myoglobins from species other than the sperm whale. Four types of T cell clones were obtained from the DBA/2 mice: 3 types responded to the peptide 107-120 (9 clones altogether), and 1 type responded to the peptide 133-149 (4 clones altogether). The 3 types responding to the peptide 107-120 could be distinguished by their response to horse myoglobin or by the restriction of the response (Ad vs. Ed). Similarly, 5 types of T cell clones were obtained from the C57BL/6 mice: 2 types responded to the peptide 10-22 (1 type, but not the other, responded to horse myoglobin); 1 type responded to the peptide 133-149; and 2 types did not respond to any of the peptides used (1 type, but not the other, responded to dog myoglobin). All 5 types (13 clones altogether) were presumably Ab restricted. These results demonstrate the diversity of epitopes in single antigenic regions and show equivalent heterogeneity of T cell repertoires in high and low responder mice. Attempts to demonstrate specific T cell suppression in the low responder mice failed; only partial, nonspecific suppression was observed.

Animals↗
PubMed1990

Crystal structure of myoglobin from a synthetic gene.

Crystals have been grown of myoglobin produced in Escherichia coli from a synthetic gene, and the structure has been solved to 1.9 A resolution. The space group of the crystals is P6, which is different from previously solved myoglobin crystal forms. The synthetic myoglobin is essentially identical to myoglobin isolated from sperm whale tissue, except for the retention of the initiator methionine at the N-terminus and the substitution of asparagine for aspartic acid at position 122. Superposition of the coordinates of native and synthetic sperm whale myoglobins reveals only minor changes in the positions of main chain atoms and reorientation of some surface side chains. Crystals of variants of the "synthetic" myoglobin have also been grown for structural analysis of the role of key amino acid residues in ligand binding and specificity.

Escherichia coli↗
PubMed2006

Compound-specific stable carbon isotope ratios (delta13C values) of the halogenated natural product 2,3,3',4,4',5,5'-heptachloro-1'-methyl-1,2'-bipyrrole (Q1).

Compound-specific isotope analysis using gas chromatography interfaced to isotope ratio mass spectrometry (GC/IRMS) was applied for the determination of delta13C values of the marine halogenated natural product 2,3,3',4,4',5,5'-heptachloro-1'-methyl-1,2'-bipyrrole (Q1). The delta13C value of a lab-made Q1 standard (-34.20 +/- 0.27 per thousand) was depleted in 13C by more than 11 per thousand relative to the residues of Q1 in dolphin blubber from Australia and skua liver from Antarctica. This clarified that the synthesized Q1 was not the source for Q1 in the biota samples. However, two Australian marine mammals showed a large variation in the delta13C value, which, in our experience, was implausible. Since the GC/IRMS system was connected to a conventional ion trap mass spectrometer by a post-column splitter, we were able to closely inspect the peak purity of Q1 in the respective samples. While the mass spectra of Q1 did not indicate any impurity, a fronting peak of PCB 101 was identified in one sample. This interference falsified the delta13C value of the respective sample. Once this sample was excluded, we found that the delta13C values of the remaining samples, i.e. liver of Antarctic brown skua (-21.47 +/- 1.47 per thousand) and blubber of Australian melon-headed whale (-22.80 +/- 0.33 per thousand), were in the same order. The standard deviation for Q1 was larger in the skua samples than in the standard and the whale blubber sample. This was due to lower amounts of skua sample available. It remained unclear if the Q1 residues originate from the same producer and location.

Adipose Tissue↗
PubMed1999

Size limitations in semicircular duct systems

The present article discusses mechanical requirements and limitations which are applicable to the construction of the system of semicircular ducts, especially to its size. The simplified case of a single, uniform duct system has been considered which can be described by a second order equation of motion. The principal functional quantities for this rotation-sensor are: (1) response speed; (2) sensitivity; and (3) regular flow. The response speed of a single, uniform semicircular duct is characterized by the short time constant (T2) which is dependent on the duct radius (r). Its estimated range is from 0.04 ms in the smallest to 140 ms in the largest known labyrinth. The sensitivity is characterized by the maximal endolymph displacement after a step stimulus (xmax). Its estimated range is from 0.0016 &mgr;m to 5.97 mm (6.56 decades!), assuming an input angular velocity of omega=1 rad s-1. The Reynolds number is a measure for an undisturbed laminar flow. Its estimated range varies from 7.38.10(-4)to 45.1 for omega=1 rad s-1. The above data follow from graphs in which, for a single uniform duct, circuit radius (R) is plotted against duct radius (r) for labyrinths of 233 species belonging to different vertebrate-groups. A relation R =38.9. r1.60was determined. The smallest labyrinth was found in a carp larva (Cyprinus), the largest in a whale shark (Rhincodon). Large whales possess labyrinths of average mammalian size. It is revealed that semicircular duct size is bound by requirements concerning regular flow and by a too low response speed for large labyrinths, and by a too low sensitivity for small labyrinths. Other important quantities are mechanical amplification factors which are a consequence of more complex vestibular constructions than a single uniform duct circuit. Allometric relationships are interpreted as compromises between the quantities mentioned. A hypothesis for the relatively large semicircular duct sizes of fishes, especially Elasmobranchii, compared with mammals and birds is presented. Copyright 1999 Academic Press.

Journal Article↗
PubMed1991

The amino acid sequence of hemoglobin II from the symbiont-harboring clam Lucina pectinata.

The cytoplasmic hemoglobin II from the gill of the clam Lucina pectinata consists of 150 amino acid residues, has a calculated Mm of 17,476, including heme and an acetylated N-terminal residue. It retains the invariant residues Phe 44 at position CD1 and His 65 at the proximal position F8, as well as the highly conserved Trp 15 at position A12 and Pro 38 at position C2. The most likely candidate for the distal residue at position E7, based on the alignment with other globins, is Gln 65. However, optical and EPR spectroscopic studies of the ferri Hb II (Kraus, D. W., Wittenberg, J. B., Lu, J. F., and Peisach, J., J. Biol. Chem. 265, 16054-16059, 1990) have implicated a tyrosinate oxygen as the distal ligand. Modeling of the Lucina Hb II sequence, using the crystal structure of sperm whale aquometmyoglobin, showed that Tyr 30 substituting for the Leu located at position B10 can place its oxygen within 2.8 A of the water molecule occupying the distal ligand position. This structural alteration is facilitated by the coordinate mutation of the residue at position CD4, from Phe 46 in the sperm whale myoglobin sequence to Leu 47 in Lucina Hb II.

Amino Acid Sequence↗
PubMed1989

Critical evaluation of polychlorinated biphenyl toxicity in terrestrial and marine mammals: increasing impact of non-ortho and mono-ortho coplanar polychlorinated biphenyls from land to ocean.

Residues of potentially toxic non-ortho chlorine substituted coplanar 3,3',4,4'-tetra-,3,3',4,4',5-penta-, 3,3',4,4',5,5'-hexachlorobiphenyl and their mono- and di-ortho analogs 2,3',4,4',5-penta, 2,3,3',4,4'-penta-, 2,3,3',4,4',5-hexa- and 2,2',3,3',4,4'-hexa-, 2,2',3,4,4',5-hexachlorobiphenyl) were determined in humans, dogs, cats (terrestrial), a finless porpoise (Neophocoena phocoenoides--coastal), Dall's porpoises (Phocoenoides dalli, dalli), Baird's beaked whales (Berardius bairdii) and killer whales (Orcinus orca--open ocean). Among the coplanar polychlorinated biphenyl (PCB) congeners, the concentration of the di-ortho congeners was the highest and the non-ortho congeners was the lowest. However, all three coplanar PCBs occurred at significantly higher levels than toxic polychlorinated dibenzo-p-dioxins (PCDDs) and polychlorinated dibenzofurans (PCDFs). The relative bioconcentration and metabolic capacity of terrestrial and marine mammals to these chemicals, suggest that the toxic threat of coplanar PCBs increases from land to ocean, but the reverse is true for PCDDs and PCDFs. The toxic threat of coplanar PCBs to higher aquatic predators such as cetaceans was principally assessed by 2,3,7,8-T4CDD Toxic Equivalent Analysis which is based on the induction of arylhydrocarbon hydroxylase (AHH) and ethoxyresorufin O-deethylase (EROD). Analysis indicates, in particular, that the bioaccumulation of toxic 3,3',4,4',5-penta- and 2,3,3',4,4'-pentachlorobiphenyls in carnivorous marine mammals is a cause for considerable concern.

Animals↗
PubMed1996

The mitochondrial DNA molecule of Sumatran orangutan and a molecular proposal for two (Bornean and Sumatran) species of orangutan.

The complete mitochondrial DNA (mtDNA) molecule of Sumatran orangutan, plus the complete mitochondrial control region of another Sumatran specimen and the control regions and five protein-coding genes of two specimens of Bornean orangutan were sequenced and compared with a previously reported complete mtDNA of Bornean orangutan. The two orangutans are presently separated at the subspecies level. Comparison with five different species pairs-namely, harbor seal/grey seal, horse/donkey, fin whale/blue whale, common chimpanzee/pygmy chimpanzee, and Homo/common chimpanzee-showed that the molecular difference between Sumatran and Bornean orangutan is much greater than that between the seals, and greater than that between the two chimpanzees, but similar to that between the horse and the donkey and the fin and blue whales. Considering their limited morphological distinction the comparison revealed unexpectedly great molecular difference between the two orangutans. The nucleotide difference between the orangutans is about 75% of that between Homo and the common chimpanzee, whereas the amino acid difference exceeds that between Homo and the common chimpanzee. On the basis of their molecular distinction we propose that the two orangutans should be recognized as different species, Pongo pygmaeus, Bornean orangutan, and P. abelii, Sumatran orangutan.

Animals↗
PubMed2006

New remains of the enigmatic cetartiodactyl Bugtitherium grandincisivum Pilgrim, 1908, from the upper Oligocene of the Bugti Hills (Balochistan, Pakistan).

Newly discovered fossil material of the enigmatic cetartiodactyl Bugtitherium grandincisivum from the upper Oligocene of the Bugti Member of the Chitarwata Formation in the Bugti Hills (Balochistan, Pakistan) is reported. These new specimens consist of two fragmentary muzzles (one preserving the first incisors and belonging to a juvenile) and a fragmentary right mandible with m3. The morphologies of the anterior dentition and m3 provided by these new specimens confirm the validity of the genus Bugtitherium and advocate probable anthracotheriid affinity for the genus rather than entelodontid or suoid affinities, but do not definitively close the debate about Bugtitherium's familial affinities within Cetartiodactyla. Although still poorly documented, this large-sized anthracotheriid-like cetartiodactyl is a possible key form for understanding the early evolution of hippos, and, in turn, the ancestry of whales, because of both its morphological similarities with hippos and primitive Paleogene whales and its Tethysian distribution.

Animals↗
PubMed2007

Determination of polybrominated diphenyl ethers in environmental standard reference materials.

Standard reference materials (SRMs) are valuable tools in developing and validating analytical methods to improve quality assurance standards. The National Institute of Standards and Technology (NIST) has a long history of providing environmental SRMs with certified concentrations of organic and inorganic contaminants. Here we report on new certified and reference concentrations for 27 polybrominated diphenyl ether (PBDE) congeners in seven different SRMs: cod-liver oil, whale blubber, fish tissue (two materials), mussel tissue and sediment (two materials). PBDEs were measured in these SRMs, with the lowest concentrations measured in mussel tissue (SRM 1974b) and the highest in sediment collected from the New York/New Jersey Waterway (SRM 1944). Comparing the relative PBDE congener concentrations within the samples, we found the biota SRMs contained primarily tetrabrominated and pentabrominated diphenyl ethers, whereas the sediment SRMs contained primarily decabromodiphenyl ether (BDE 209). The cod-liver oil (SRM 1588b) and whale blubber (SRM 1945) materials were also found to contain measurable concentrations of two methoxylated PBDEs (MeO-BDEs). Certified and reference concentrations are reported for 12 PBDE congeners measured in the biota SRMs and reference values are available for two MeO-BDEs. Results from a sediment interlaboratory comparison PBDE exercise are available for the two sediment SRMs (1941b and 1944).

Journal Article↗
PubMed2000

Measuring shifts in function and evolutionary opportunity using variability profiles: a case study of the globins.

Variability profiles measured over a set of aligned sequences can be used to estimate evolutionary freedom to vary. Differences in variability profiles between clades can be used to identify shifts in function at the molecular level. We demonstrate such a shift between the alpha and beta subunits of hemoglobin. We also show that the variability profiles for myoglobin are different between whales and primates and speculate that the differences between the two clades may reflect a shift associated with the novel oxygen storage demands in the lineage leading to whales. We discuss the relationship between sequence variability and "evolutionary opportunity" and explore the utility of Maynard Smith's multidimensional evolutionary opportunity space metaphor for exploring functional constraints, genetic redundancy, and the context dependency of the genotype-phenotype map. This work has implications for quantitatively defining and comparing protein function. Supplementary data is available from bioinfo.mbb.yale. edu/align.

Animals↗