The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
MeSH Review

Sperm Whale

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Sperm Whale


High impact information on Sperm Whale

  • To test these ideas, engineered mutants of sperm whale myoglobin and the alpha- and beta-subunits of human haemoglobin were prepared in which E7 histidine was replaced by glycine [3].
  • The sera from mice which received the peptide with the added sequence 105-121 from sperm whale myoglobin did not neutralize the virus, although they had high levels of anti-141-160 FMDV peptide activity [4].
  • T cell clones recognizing the sperm whale myoglobin (SpWMb) epitope 110-121 in association with H-2d major histocompatibility complex class II molecules display a very limited heterogeneity of T cell receptor (TCR) V beta usage in DBA/2 mice [5].
  • The second line of evidence that processing of native myoglobin may influence the apparent specificity of the T cell response was obtained using the I-Ad-restricted sperm whale myoglobin 102-118-specific clone 9.27 [6].
  • We determined the structure of the photolytic intermediate of a sperm whale myoglobin (Mb) mutant called Mb-YQR [Leu-(B10)-->Tyr; His(E7)-->Gln; Thr(E10)-->Arg] to 1.4-A resolution by ultra-low temperature (20 K) x-ray diffraction [7].

Biological context of Sperm Whale

  • Low-temperature flash photolysis with IR and visible spectroscopy was used to probe the influence of the distal histidine His-64(E7) of sperm-whale myoglobin (Mb) on the orientation of bound carbon monoxide (CO) and on the kinetics of CO rebinding [1].
  • These experiments demonstrate that electron transport from the Fe(II)-heme to site-specifically bound Cu(II) can be mediated through multiple pathways in sperm whale Mb [8].
  • The effects of high pressure (0.1-3.4 gigapascal (GPa)) on the ferrous heme active sites of human adult hemoglobin, sperm whale myoglobin, and Glycera dibranchiata hemoglobin (Fraction II) were probed using resonance Raman and absorption spectroscopies [9].
  • The effect of lactate on O2 binding properties of sperm whale and horse heart myoglobins (Mb) has been investigated at moderately acid pH (i.e. pH 6.5, a condition which may be achieved in vivo under a physical effort) [10].
  • 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 [11].

Anatomical context of Sperm Whale

  • Antigen-stimulated secretion of gamma-interferon (IFN-gamma) by sperm whale myoglobin-specific Th1 cells of DBA/2 mouse I-Ed-restricted clones, which express VIPR1 and VIPR2, was enhanced by 10(-10) M to 10(-7) M VIP [12].
  • 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 [13].
  • When marrow mononuclear cells were cultured on sperm whale dentine slices in the presence of 1 alpha,25-(OH)2D3 or PTH, numerous resorption lacunae were formed [14].
  • In parallel, the proliferative response of CD4+ T-cells to the primary protein antigens keyhole limpet hemocyanin (KLH) and sperm whale myoglobin (SWM) was measured in vitro using monocyte-derived dendritic cells (MDDC) as antigen-presenting cells [15].
  • This laboratory had previously mapped the regions of T and B cell recognition on sperm whale myoglobin (Mb) [16].

Associations of Sperm Whale with chemical compounds

  • Sperm whale myoglobin (Mb) reduces Cu(II) through a site-specific mechanism involving complexation by one or more surface histidine residues [8].
  • The spectrum of sperm whale oxymyoglobin is diagnostic of a bent (formula: see text) oxheme coordination geometry with totally spin-paired, ground-state electronic configurations of the iron and of the dioxygen ligand [17].
  • The vibrational energy relaxation of carbon monoxide in the heme pocket of sperm whale myoglobin was studied by using molecular dynamics simulation and normal mode analysis methods [18].
  • Sperm whale Mb and derivatives have two tryptophans and their decays can be interpreted mainly as two exponentials, one of ca. 20 ps and the other of 130 ps, whereas tuna Mb has one tryptophan and its emission is nonexponential but dominated by one component of 31 ps [19].
  • However, because sperm whale and horse myoglobin differ at this residue (glutamate vs. aspartate, respectively), T lymphocytes immune to each myoglobin do not crossreact with the other myoglobin [20].

Gene context of Sperm Whale

  • Also, binding kinetics suggest that heme binding to the PAS-B domain of NPAS2 is relatively weak compared with that of sperm whale myoglobin [21].
  • As expected, the overall structure is quite similar to the sperm whale myoglobin structure [22].
  • To examine the effect of aggregation sequence QGGYQQQYNP from yeast Sup35 on fibril formation of sperm whale apomyoglobin (apoMb), we constructed several mutants via substitution [23].
  • T cell clones reactive with sperm whale myoglobin. Isolation of clones with specificity for individual determinants on myoglobin [24].
  • Mutants of sperm whale myoglobin were constructed at position 29 (B10 in helix notation) to examine the effects of distal pocket size on the rates of ligand binding and autooxidation [25].

Analytical, diagnostic and therapeutic context of Sperm Whale


  1. Ligand binding to synthetic mutant myoglobin (His-E7----Gly): role of the distal histidine. Braunstein, D., Ansari, A., Berendzen, J., Cowen, B.R., Egeberg, K.D., Frauenfelder, H., Hong, M.K., Ormos, P., Sauke, T.B., Scholl, R. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  2. Image contrast of biological materials in high-voltage electron microscopy. Bhakat, P., Bhattacharya, D.K. Journal of electron microscopy. (1997) [Pubmed]
  3. The role of the distal histidine in myoglobin and haemoglobin. Olson, J.S., Mathews, A.J., Rohlfs, R.J., Springer, B.A., Egeberg, K.D., Sligar, S.G., Tame, J., Renaud, J.P., Nagai, K. Nature (1988) [Pubmed]
  4. Non-responsiveness to a foot-and-mouth disease virus peptide overcome by addition of foreign helper T-cell determinants. Francis, M.J., Hastings, G.Z., Syred, A.D., McGinn, B., Brown, F., Rowlands, D.J. Nature (1987) [Pubmed]
  5. The T cell receptor repertoire influences V beta element usage in response to myoglobin. Ruberti, G., Gaur, A., Fathman, C.G., Livingstone, A.M. J. Exp. Med. (1991) [Pubmed]
  6. Influences of antigen processing on the expression of the T cell repertoire. Evidence for MHC-specific hindering structures on the products of processing. Brett, S.J., Cease, K.B., Berzofsky, J.A. J. Exp. Med. (1988) [Pubmed]
  7. The role of cavities in protein dynamics: crystal structure of a photolytic intermediate of a mutant myoglobin. Brunori, M., Vallone, B., Cutruzzola, F., Travaglini-Allocatelli, C., Berendzen, J., Chu, K., Sweet, R.M., Schlichting, I. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  8. Site-directed mutagenesis of histidine residues involved in Cu(II) binding and reduction by sperm whale myoglobin. Van Dyke, B.R., Bakan, D.A., Glover, K.A., Hegenauer, J.C., Saltman, P., Springer, B.A., Sligar, S.G. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  9. The effects of high pressure upon ligated and deoxyhemoglobins and myoglobin. An optical spectroscopic study. Alden, R.G., Satterlee, J.D., Mintorovitch, J., Constantinidis, I., Ondrias, M.R., Swanson, B.I. J. Biol. Chem. (1989) [Pubmed]
  10. Functional modulation by lactate of myoglobin. A monomeric allosteric hemoprotein. Giardina, B., Ascenzi, P., Clementi, M.E., De Sanctis, G., Rizzi, M., Coletta, M. J. Biol. Chem. (1996) [Pubmed]
  11. 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. Twining, S.S., Lehmann, H., Atassi, M.Z. Biochem. J. (1980) [Pubmed]
  12. Enhancement by vasoactive intestinal peptide of gamma-interferon production by antigen-stimulated type 1 helper T cells. Jabrane-Ferrat, N., Bloom, D., Wu, A., Li, L., Lo, D., Sreedharan, S.P., Turck, C.W., Goetzl, A.E. FASEB J. (1999) [Pubmed]
  13. Properties of monoclonal antibodies specific for determinants of a protein antigen, myoglobin. Berzofsky, J.A., Hicks, G., Fedorko, J., Minna, J. J. Biol. Chem. (1980) [Pubmed]
  14. Osteoclast-like cell formation and its regulation by osteotropic hormones in mouse bone marrow cultures. Takahashi, N., Yamana, H., Yoshiki, S., Roodman, G.D., Mundy, G.R., Jones, S.J., Boyde, A., Suda, T. Endocrinology (1988) [Pubmed]
  15. Impaired primary immune response in type-1 diabetes: results from a controlled vaccination study. Eibl, N., Spatz, M., Fischer, G.F., Mayr, W.R., Samstag, A., Wolf, H.M., Schernthaner, G., Eibl, M.M. Clin. Immunol. (2002) [Pubmed]
  16. B-cell activation in vitro by helper T cells specific to a protein region that is recognized both by T cells and by antibodies. Hamajima, S., Atassi, M.Z. Immunol. Invest. (1998) [Pubmed]
  17. Fe-O2 bonding and oxyheme structure in myoglobin. Makinen, M.W., Churg, A.K., Glick, H.A. Proc. Natl. Acad. Sci. U.S.A. (1978) [Pubmed]
  18. Vibrational population relaxation of carbon monoxide in the heme pocket of photolyzed carbonmonoxy myoglobin: comparison of time-resolved mid-IR absorbance experiments and molecular dynamics simulations. Sagnella, D.E., Straub, J.E., Jackson, T.A., Lim, M., Anfinrud, P.A. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  19. Picosecond fluorescence decay of tryptophans in myoglobin. Hochstrasser, R.M., Negus, D.K. Proc. Natl. Acad. Sci. U.S.A. (1984) [Pubmed]
  20. A possible immunodominant epitope recognized by murine T lymphocytes immune to different myoglobins. Berkower, I., Buckenmeyer, G.K., Gurd, F.R., Berzofsky, J.A. Proc. Natl. Acad. Sci. U.S.A. (1982) [Pubmed]
  21. Spectroscopic characterization of the isolated heme-bound PAS-B domain of neuronal PAS domain protein 2 associated with circadian rhythms. Koudo, R., Kurokawa, H., Sato, E., Igarashi, J., Uchida, T., Sagami, I., Kitagawa, T., Shimizu, T. FEBS J. (2005) [Pubmed]
  22. X-ray crystal structure of a recombinant human myoglobin mutant at 2.8 A resolution. Hubbard, S.R., Hendrickson, W.A., Lambright, D.G., Boxer, S.G. J. Mol. Biol. (1990) [Pubmed]
  23. Fibrillogenesis of apomyoglobin facilitated by aggregation sequence of yeast Sup35 in various regions. He, Y., Tang, H., Yi, Z., Zhou, H., Luo, Y. FEBS Lett. (2005) [Pubmed]
  24. T cell clones reactive with sperm whale myoglobin. Isolation of clones with specificity for individual determinants on myoglobin. Infante, A.J., Atassi, M.Z., Fathman, C.G. J. Exp. Med. (1981) [Pubmed]
  25. A novel site-directed mutant of myoglobin with an unusually high O2 affinity and low autooxidation rate. Carver, T.E., Brantley, R.E., Singleton, E.W., Arduini, R.M., Quillin, M.L., Phillips, G.N., Olson, J.S. J. Biol. Chem. (1992) [Pubmed]
  26. Titration behavior of individual tyrosine residues of myoglobins from sperm whale, horse, and red kangaroo. Wilbur, D.J., Allerhand, A. J. Biol. Chem. (1976) [Pubmed]
  27. Reduction of sperm whale ferrylmyoglobin by endogenous reducing agents: potential reducible loci of ferrylmyoglobin. Arduini, A., Mancinelli, G., Radatti, G.L., Damonti, W., Hochstein, P., Cadenas, E. Free Radic. Biol. Med. (1992) [Pubmed]
  28. Identification of the myoglobin tyrosyl radical by immuno-spin trapping and its dimerization. Detweiler, C.D., Lardinois, O.M., Deterding, L.J., de Montellano, P.R., Tomer, K.B., Mason, R.P. Free Radic. Biol. Med. (2005) [Pubmed]
  29. Crystal structures of CO-, deoxy- and met-myoglobins at various pH values. Yang, F., Phillips, G.N. J. Mol. Biol. (1996) [Pubmed]
WikiGenes - Universities