Анализ комплексов лактоферрина молока человека
Дипломная работа - Химия
Другие дипломы по предмету Химия
esolution. Refinement and analysis of ligand-induced conformational change (1998) Acta Crystallogr. D. Biol. Crystallogr., 54, 1319-1335., D., Salmon, V., Coddeville, B., Benaissa, M., Plancke, Y., Spik, G. Structural determination of two N-linked glycans isolated from recombinant human lactoferrin expressed in BHK cells (1995) FEBS Lett., 365(1), 57-60.Berkel, P.H., van Veen, H.A., Geerts, M.E., de Boer, H.A., Nuijens, J.H. Heterogeneity in utilization of N-glycosylation sites Asn624 and Asn138 in human lactoferrin: a study with glycosylation-site mutants (1996) Biochem. J., 319, 117-122.Berkel, P.H., Geerts, M.E., van Veen, H.A., Kooiman, P.M., Pieper, F.R., de Boer, H.A., Nuijens, J.H. Glycosylated and unglycosylated human lactoferrins both bind iron and show identical affinities towards human lysozyme and bacterial lipopolysaccharide, but differ in their susceptibilities towards tryptic proteolysis (1995) Biochem. J., 312, 107-114., N., Retequi, L., Masson, P. . Comprasion on human lactoferrins from milk and neutrophilic leucocytes. Relative molecular mass, isoelectric point, iron-binding properties and uptake by the liver. (1985) Biochem. J., 229, 353-359., M.S., Smith, C.A., Ainscough, E.C., Baker, H.A., Brodie, A.M., Baker, E.N. Anion binding by human lactoferrin: results from crystallographic and physicochemical studies. (1992) Biochem. J., 31, 4451-4458. , L. A., and Lonnerdal, B. Fe-saturation and proteolysis of human lactoferrin: effect on brush-border receptor-mediated uptake of Fe and Mn. 1989 Dec;257(6 Pt 1):G930-4. J., SpikG. Comparative study of the iron-binding properties of human transferring. Complete and sequential iron saturation and desaturation of the lactotransferrin. 1980 Biochim. Biophys. Acta, 629, 399-408., M., Brock, J.H., Iron in immunity. Cancer and Inflammation (1989) John Wiley & Sons., R.M., Bagby, G.C., Davis, J. (1981) Calcium-dependent polymerization of lactoferrin Biochem. Biophys. Res. Commun., 101(1), 88-95., G.C.Jr., Bennett, R.M. Feedback regulation of granulopoiesis: polymerization of lactoferrin abrogates its ability to inhibit CSA production (1982) Blood, 60(1), 108-112., C., Miyazawa, K., Broxmeyer, H.E. Physical characteristics and polymerization during iron saturation of lactoferrin, a myelopoietic regulatory molecule with suppressor activity (1994) Adv. Exp. Med. Biol., 357, 121-132., A., Kuyas, C., Haeberli, A. Oxidative radioiodination damage to human lactoferrin. (1986) Biochem. J., 240, 239-245.
Semenov, D.V., Kanyshkova, T.G., Buneva, V.N., Nevinsky, G.A. Human milk lactoferrin binds ATP and dissociates into monomers. (1999) Biochem. Mol. Biol. Int., 47(2), 177-84., J.H. N-terminal stretch Arg2, Arg3, Arg4 and Arg5 of human lactoferrin is essential for binding to heparin, bacterial lipopolysaccharide, human lysozyme and DNA. (1997) Biochem. J., 328, 145-151)
He, J., Furmanski, P. Sequence specificity and transcriptional activation in the binding of lactoferrin to DNA. (1995) Nature, 373, 721-724.
Kanyshkova, T.G., Semenov, D.V., Buneva, V.N., Nevinsky, G.A. Human milk lactoferrin binds two DNA molecules with different affinities. (1999) FEBS Lett., 451, 235-237S.E., Nevinsky G.A. Lactoferrin interacts with nucleotides. Nucleosides Nucleotides Nucleic Acids. 2004. 23(6&7), 1043-1046
Georgy A. Nevinsky and Svetlana E. Babina. Human lactoferrin and its polyfunctional biological functions. In Protein Structure. Kaleidoscope of Structural Properties and Functions (Ed. V. N. Uversky), Research Signpost, 2003, 499-530
Furmanski, P., Li, Z.P., Fortuna, M.B., Swamy, C.V., Das, M.R. Multiple molecular forms of human lactoferrin. Identification of a class of lactoferrins that possess ribonuclease activity and lack iron-binding capacity (1989) J. Exp. Med., 170, 415-429.
Furmanski, P., Li, Z.P. Multiple forms of lactoferrin in normal and leukemic human granulocytes. (1990) Exp. Hematol. 18(8), 932-935.T.G., Babina S.E., Semenov D.V., Isaeva N., Vlassov A.V., Neustroev K.N., Kulminskaya A.A., Buneva V.N., Nevinsky G.A. Multiple enzymic activities of human milk lactoferrin. Eur. J. Biochem. 2003. V. 270. P. 3353-3361.
Бабина С.Е., Канышкова Т.Г., Бунева В.Н., Невинcкий Г.А. Лактоферрин - дезоксирибонуклеаза человеческого молока. Биохимия. 2004. 69(9), 1239-1250.
Бабина С.Е., Семенов Д.И., Бунева В.Н., Невинcкий Г.А. Лактоферрин грудного молока гидролизует рибонуклеозид-5-трифосфаты. Молекуляр. биол., 2005. 39(3), 513-520.F.V., Zinoviev V.V., Vavilin V.I. and Malygin E.G. Application of the Small-Angle X-ray Scattering technique for the study of two-step equilibrium enzyme-substrate interactions. Biopolymers. 1996. V.38. P.131-139.31
Гилл Ф., Мюррей У., Райт М. 1985. Практическая оптимизация. М.: Мир., 509с.
Тузиков Ф.В. Анализ биологических наноструктур в системах метаболизма белков и липидов: строение, дисперсный состав и механизмы равновесных взаимодействий макромолекул. Дисс. на соиск. уч. степ. д.б.н. 20005. Новосибирск. 364с.