Some properties of a macromolecular conjugate of lysozyme prepared by modification with a monomethoxypolyethylene glycol derivative

Bioscience, Biotechnology and Biochemistry

Volumn 64, Issue 4, 2000, Pages 767-774

  Nodake, Yuichi ^a   Yamasaki, Nobuyuki ^a  

^a KYUSHU UNIVERSITY   (Japan)

Author keywords

Hen egg white lysozyme; Immunogenicity; Monomethoxypolyethylene glycol (mPEG); Protein polymer conjugate; Thermostability

Indexed keywords

LYSOZYME; MACROGOL DERIVATIVE; MONOMETHOXYPOLYETHYLENE GLYCOL;

ANIMAL; ARTICLE; BAGG ALBINO MOUSE; CHEMISTRY; CIRCULAR DICHROISM; ENZYME STABILITY; HEATING; HUMAN; ISOLATION AND PURIFICATION; MACROMOLECULE; METABOLISM; MOUSE; SPECTROFLUOROMETRY;

ANIMALS; CIRCULAR DICHROISM; ENZYME STABILITY; HEATING; HUMANS; MACROMOLECULAR SUBSTANCES; MICE; MICE, INBRED BALB C; MURAMIDASE; POLYETHYLENE GLYCOLS; SPECTROMETRY, FLUORESCENCE;

MICROCOCCUS LUTEUS;

EID: 0034169308     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.64.767     Document Type: Article

References (28)

1. Abuchowski, A., van Es T., Palczuk, N. C., and Davis, F. F., Alteration of immunological properties of bovine serum albumin by covalent attachment of polyethylene glycol. J. Biol. Chem., 252, 3578-3581 (1977).
2. Wie, S. I., Wie, C. W., Lee, W. Y., Filion, L. G., Sehon, A. H., and Akerbiom, E., Suppression of rea-ginic antibodies with modified allergens. III. Preparation of tolerogenic conjugates of common allergens with monomethoxypolyethylene glycols of different molecular weights by the mixed anhydride method. Int. Arch. Allergy Appl. Immunol., 64, 84-99 (1981).
3. Inada, Y., Nishimura, FI., Takahashi, K., Yoshimoto, T., Saha, A. R., and Saito, Y., Ester synthesis catalyzed by polyethylene glycol-modified lipase in benzene. Biochem. Biophys. Res. Commun., 122, 845-850 (1984).
4. Yamasaki, N., Matsuo, A., and Isobe, H., Novel polyethylene glycol derivatives for modification of proteins. Agric. Biol. Chem., 52, 2125-2127 (1988).
5. Hershfield, M. S., Buckley, R. H., Greenberg, M. L., Melton, A. L., Schiff, R., Hatem, C., Kurtzberg, J., Markert, M. L., Kobayashi, R. H., Kobayashi, A. L., and Abuchowski, A., Treatment of adenosine deaminase deficiency with polyethylene glycol-modified adenosine deaminase. N. Engl. J. Med., 316, 589-596 (1987).
6. Jurgens, H., Schwamborn, D., Korholz, D., Wahn, V., and Gobel, U., Clinical experiences with polyethylene glycol-bound E. coli L-asparaginase in patients with multiple recurrences of acute lymphoblastic leukemia. Klin. Padiatr., 200, 184-189 (1988).
7. Sugi, K., Inoue, M., and Morino, Y., Degradation of plasma bilirubin by a bilirubin oxidase derivative which has a relatively long half-life in the circulation. Biochim. Biophys. Acta, 991, 405-409 (1989).
8. Kuan, C. T., Wang, Q., and Pastan, I., Pseudomonas exotoxin A mutants. Replacement of surface exposed residues in domain II with cysteine residues that can be modified with polyethylene glycol in a site-specific manner. J. Biol. Chem., 269, 7610-7616 (1994).
9. Yamasaki, N., Matsuo, A., Hatakeyama, T., and Funatsu, G., Some properties of ricin D modified with a methoxypolyethylene glycol derivative. Agric. Biol. Chem., 54, 2635-2640 (1990).
10. Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
11. Fields, R., The measurement of amino groups in proteins and peptides. Biochem. J., 124, 581-590 (1971).
12. Crestifield, 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).
13. Heinrikson, R. L. and Meredith, S. C., Amino acid analysis by reverse-phase high-performance liquid chromatography: precolumn derivatization with phenylisothiocyanate. Anal. Biochem., 136, 65-74 (1984).
14. Imoto, T. and Yagishita, K., A simple activity measurement of lysozyme. Agric. Biol. Chem., 35, 1154-1156 (1971).
15. Smolelis, A. N. and Flartsell, S. E., Factors affecting the lytic activity of lysozyme. J. Bacteriol., 63, 665-674 (1952).
16. Ichikawa, A., Tachibana, FI., Kawamoto, S., Kamei, M., Honjoh, T., Hashizume, S., and Shirahata, S., Cytokeratin 8 and 19 as antigens recognized by adenocarcinoma-reactive human monoclonal antibody AE6F4. Human Antibodies, 8, 195-202 (1997).
17. Swank, R. T. and Munkers, K. D., Molecular weight analysis of oligopeptides by electrophoresis in polyacrylamide gel with sodium dodecyl sulfate. Anal. Biochem., 39, 462-477 (1971).
18. Canfield, R. E., The amino acid sequence of egg white lysozyme. J. Biol. Chem., 238, 2698-2707 (1963).
19. Veerapandian, B., Salunke, D. M., and Vijayan, M., X-ray characterisation of an additional binding site in lysozyme. FEBS Lett., 186, 163-167 (1985).
20. Yamada, H., Matsunaga, N., Domoto, FF, and Imoto, T., Dinitrophenylation as a probe for the determination of environments of amino groups in protein. Reactivities of individual amino groups in lysozyme. J. Biochem., 100, 233-241 (1986).
21. Blake, C. C. F., Johnson, L. N., Mair, G. A., North, A. C. T., Philips, D. C., and Sarma, V. R., Crystallographic studies of the activity of hen egg-white lysozyme. Proc. R. Soc., Fond., B167, 378-388 (1967).
22. Yamasaki, N., Hayasi, K., and Funatsu, M., Acetylation of lysozyme Part I. Preparation, Fractionation and properties of acetylated lysozyme. Agric. Biol. Chem., 32, 55-63 (1968).
23. Yamasaki, N., Hayasi, K., and Funatsu, M., Acetylation of lysozyme Part II. Mechanism of lysis by lysozyme. Agric. Biol. Chem., 32, 64-68 (1968).
24. Liu, K. J. and Persons, J. L., Solvent effects on the preferred conformation of polyethylene glycols. Macromolecules, 2, 529-533 (1969).
25. Atassi, M. Z., Precise determination of the entire antigenic structure of lysozyme. Immunochemistry, 15, 909-936 (1978).
26. David, R., Davies, S. S., and Eduardo, A. P., Antibody-Antigen Complexes. J. Biol. Chem., 263, 10541-10544 (1963).
27. Yoshimoto, T., Chao, S. G., Saito, Y., Imamura, I., Wada, H., and Inada, Y., Chemical modification of tryptophanase from E. coli with polyethylene glycol to reduce its immunoreactivity towards anti-tryp-tophanase antibodies. Enzime, 36, 261-265 (1986).
28. Lee, K. C., Moon, S. C., Park, M. O., Lee, J. T., Na, D. H., Yoo, S. D., Lee, H. S., and DeLuca, P. P., Isolation, characterization, and stability of positional isomers of mono-PEGylated salmon calcitonins. Pharmaceutical Research, 16, 813-818 (1999).