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Original Articles

The Amino Acid Sequence of Monal Pheasant Lysozyme and Its Activity

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Pages 1988-1994 | Received 14 May 1998, Published online: 22 May 2014

  • 1) Canfield, R. E., The amino acid sequence of egg white lysozyme. J. Biol. Chem., 238, 2698-2707 (1963).
  • 2) Simpson, R. J. Begg, G. S., Dorow, D. S., and Morgan, F. J., Complete amino acid sequence of the goose-type lysozyme from the egg white of the black swan. Biochemistry, 19, 1814-1819 (1980).
  • 3) Inoue, M., Imada, M., and Tsugita, A., The amino acid sequence of T4 phage lysozyme. IV. Dilute acid hydrolysis and the order of tryptic peptides. J. Biol. Chem., 245, 3479-3484 (1970).
  • 4) Canfield, R. E., Kammerman, S., Sobel, H. H., and Morgan, F. J., Primary structure of lysozymes from man and goose. Nature, 232, 16-17 (1971).
  • 5) Dautigny, A., Prager, E. M., Pham-Dinh, D., Jollés, J., Pakdel, F., Grinde, B., and Jollés, P., cDNA and amino acid sequences of rainbow trout (Oncorhynchus mykiss) lysozymes and their implications for the evolution of lysozyme and lactalbumin. J. Mol. Evol., 32, 187-198 (1991).
  • 6) Daffre, S., Kylsten, P., Samakovlis, C., and Hultmark, D., The lysozyme locus in Drosophila melanogaster: an expanded gene family adapted for expression in the digestive tract. Mol. Gen. Genet., 242, 152-162 (1994).
  • 7) Engstrom, A., Xanthopoulos, K. G., Boman, H. G., and Bennich, H., Amino acid and cDNA sequence of lysozyme from Hyalophora cecropia. EMBO J., 4, 2119-2122 (1985).
  • 8) Prager, E. M., Wilson, A. C., and Arnheim, N., Widespread distribution of lysozyme g in egg white of birds. J. Biol. Chem., 249, 7295-7294 (1974).
  • 9) Jollés, J., Jauregui-Adell, J., Bernier, I., and Jollés, P., La structure chimique du lysozyme de blanc d’oeuf de poule: étude détaillée. Biochim. Biophys. Acta, 78, 668-689 (1963).
  • 10) Jung, A., Sippel, A. E., Grez, M., and Schutz, G., Exons encode functional and structural units of chicken lysozyme. Proc. Natl. Acad. Sci. U.S.A., 77, 5759-5763 (1980).
  • 11) LaRue, J. N. and Speck Jr., J. C., Turkey egg white lysozyme. Preparation of the crystalline enzyme and investigation of the amino acid sequence. J. Biol. Chem., 245, 1985-1991 (1970).
  • 12) Prager, E. M., Arnheim, N., Mross, G. A., and Wilson, A. C., Amino acid sequence studies on bobwhite quail egg white lysozyme. J. Biol. Chem., 247, 2905-2916 (1972).
  • 13) Ibrahimi, I. M., Prager, E. M., White, T. J., and Wilson, A. C., Amino acid sequence of California quail lysozyme. Effect of evolutionary substitutions on the antigenic structure of lysozyme. Biochemistry, 18, 2736-2744 (1979).
  • 14) Kaneda, M., Kato, I., Tominaga, N., Titani, K., and Narita, K., The amino acid sequence of quail lysozyme. J. Biochem., 66, 747-749 (1969).
  • 15) Jollés, J., Ibrahimi, I. M., Prager, E. M., Schoentgen, F., Jollés, P., and Wilson, A. C., Amino acid sequence of pheasant lysozyme. Evolutionary change affecting processing of prelysozyme. Biochemistry, 18, 2744-2752 (1979).
  • 16) Araki, T., Kuramoto, M., and Torikata, T., Study of the Japanese pheasant egg white lysozyme. II. Amino acid sequence of Japanese pheasant egg white lysozyme. Proc. Facul. Agric. Kyushu Tokai Univ. (in Japanese), 7, 81-86 (1988).
  • 17) Araki, T., Kuramoto, M., and Torikata, T., The amino acid sequence of Lady Amherst’s pheasant (Chrysolophus amherstiae) and golden pheasant (Chrysolophus pictus) egg-white lysozymes. Agric. Biol. Chem., 54, 2299-2308 (1990).
  • 18) Araki, T., Kudo, K., Kuramoto, M., and Torikata, T., The amino acid sequence of lysozyme from kalij pheasant egg-white. Agric. Biol. Chem., 55, 1701-1706 (1991).
  • 19) Araki, T., Kuramoto, M., and Torikata, T., The amino acid sequence of reeves’ pheasant lysozyme. Agric. Biol. Chem., 55, 1707-1713 (1991).
  • 20) Araki, T., Kudo, K., Kuramoto, M., and Torikata, T., The amino acid sequence of Indian peafowl (Pavo cristatus) lysozyme and its comparison with lysozymes from phasianoid birds. Agric. Biol. Chem., 53, 2955-2962 (1989).
  • 21) Jollés, J., van Leemputten, E., Mouton, A., and Jollés, P., Amino acid sequence of guinea-hen egg-white lysozyme. Biochim. Biophys. Acta, 257, 497-510 (1972).
  • 22) Araki, T., Kuramoto, M., and Torikata, T., The amino acid sequence of copper pheasant lysozyme. Biosci. Biotechnol. Biochem., 58, 794-795 (1994).
  • 23) Masaki, A., Fukamizo, T., Otakara, A., Torikata, T., Hayashi, K., and Imoto, T., Estimation of rate constants in lysozyme-catalyzed reaction of chitooligosaccharides. J. Biochem., 90, 1167-1175 (1981)
  • 24) Fukamizo, T., Minematsu, T., Yanase, Y., Hayashi, K., and Goto, S., Substrate size dependence of lysozyme-catalyzed reaction. Arch. Biochem. Biophys., 250, 312-321 (1986)
  • 25) Fukamizo, T., Goto, S., Torikata, T., and Araki, T., Enhancement of transglycosilation activity of lysozyme by chemical modification. Agric. Biol. Chem., 53, 2641-2651 (1989)
  • 26) Araki, T., Yamamoto, T., and Torikata, T., Reptile Lysozyme: The complete amino acid sequence of soft-shelled turtle lysozyme and its activity. Biosci. Biotechnol. Biochem., 62, 316-324 (1998).
  • 27) Crestfield, A. M., Moore, S., and Stein, W. H., The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins. J. Biol. Chem., 238, 622-627 (1963).
  • 28) Chang, J. Y., Brauer, D., and Wittmann-Liebold, B., Micro -sequence analysis of peptides and proteins using 4-NN-dimethylaminoazobenzene 4′-isothiocyanate/phenylisothiocyanate double coupling method. FEBS Lett., 93, 205-214 (1978).
  • 29) Yang, C. Y., Die trennung der 4-[4-(dimethylamino)phenylazo]phenylthiohydantoin-derivate des leucins und isoleucins uber polyamid-dunnschichtplatten im picomol-bereich. Hoppe-Seyler’s Z. Physiol. Chem., 360, 1673-1675 (1979).
  • 30) Hein, J., A new method that simultaneously aligns and reconstructs ancestral sequences for any number of homologous sequences, when the phylogeny is given. Mol. Biol. Evol., 6, 649-668 (1989).
  • 31) Hein, J., A tree reconstruction method that is economical in the number of pairwise comparisons used. Mol. Biol. Evol., 6, 669-684 (1989).

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