Abstract
Glutathione synthetase of Escherichia coli B was modified with polyethylene glycol, and the properties of the resultant modified enzyme were investigated. The thermal stability of the modified enzyme and its resistance against several proteases increased compared with those of the native enzyme. The modified enzyme was injected intravenously via the rat tail vein, and the circulating life of the enzyme in plasma was monitored. The half-life of the native enzyme was 50 min, whereas that of the modified enzyme was approximately 24 h. The systemic anaphylaxis reaction was tested by using rats intravenously injected with the native and modified enzymes. For the native enzyme, strong reactions such as dyspnea and tumble were observed; however, no symptom or only a very weak reaction, such as scratching, was observed with the modified enzyme.
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- Barton N. W., Furbish F. S., Murray G. J., Garfield M., Brady R. O. Therapeutic response to intravenous infusions of glucocerebrosidase in a patient with Gaucher disease. Proc Natl Acad Sci U S A. 1990 Mar;87(5):1913–1916. doi: 10.1073/pnas.87.5.1913. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Berger E. A., Fuerst T. R., Moss B. A soluble recombinant polypeptide comprising the amino-terminal half of the extracellular region of the CD4 molecule contains an active binding site for human immunodeficiency virus. Proc Natl Acad Sci U S A. 1988 Apr;85(7):2357–2361. doi: 10.1073/pnas.85.7.2357. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Beutler E., Lisker R., Kuhl W. Molecular biology of G 6 PD variants. Biomed Biochim Acta. 1990;49(2-3):S236–S241. [PubMed] [Google Scholar]
- Bory C., Boulieu R., Souillet G., Chantin C., Guibaud P., Hershfield M. S. Effect of polyethylene glycol-modified adenosine deaminase (PEG-ADA) therapy in two ADA-deficient children: measurement of erythrocyte deoxyadenosine triphosphate as a useful tool. Adv Exp Med Biol. 1991;309A:173–176. doi: 10.1007/978-1-4899-2638-8_39. [DOI] [PubMed] [Google Scholar]
- Brosius J., Holy A. Regulation of ribosomal RNA promoters with a synthetic lac operator. Proc Natl Acad Sci U S A. 1984 Nov;81(22):6929–6933. doi: 10.1073/pnas.81.22.6929. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gushima H., Yasuda S., Soeda E., Yokota M., Kondo M., Kimura A. Complete nucleotide sequence of the E. coli glutathione synthetase gsh-II. Nucleic Acids Res. 1984 Dec 21;12(24):9299–9307. doi: 10.1093/nar/12.24.9299. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Haber E., Quertermous T., Matsueda G. R., Runge M. S. Innovative approaches to plasminogen activator therapy. Science. 1989 Jan 6;243(4887):51–56. doi: 10.1126/science.2492113. [DOI] [PubMed] [Google Scholar]
- Hershfield M. S., Chaffee S., Koro-Johnson L., Mary A., Smith A. A., Short S. A. Use of site-directed mutagenesis to enhance the epitope-shielding effect of covalent modification of proteins with polyethylene glycol. Proc Natl Acad Sci U S A. 1991 Aug 15;88(16):7185–7189. doi: 10.1073/pnas.88.16.7185. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hibi T., Kato H., Nishioka T., Oda J., Yamaguchi H., Katsube Y., Tanizawa K., Fukui T. Use of adenosine (5')polyphospho(5')pyridoxals to study the substrate-binding region of glutathione synthetase from Escherichia coli B. Biochemistry. 1993 Feb 16;32(6):1548–1554. doi: 10.1021/bi00057a020. [DOI] [PubMed] [Google Scholar]
- Inoue Y., Kimura A. Methylglyoxal and regulation of its metabolism in microorganisms. Adv Microb Physiol. 1995;37:177–227. doi: 10.1016/s0065-2911(08)60146-0. [DOI] [PubMed] [Google Scholar]
- Inoue Y., Tran L. T., Kamakura M., Izawa S., Miki T., Tsujimoto Y., Kimura A. Oxidative stress response in yeast: glutathione peroxidase of Hansenula mrakii is bound to the membrane of both mitochondria and cytoplasm. Biochim Biophys Acta. 1995 Dec 14;1245(3):325–330. doi: 10.1016/0304-4165(95)00117-4. [DOI] [PubMed] [Google Scholar]
- Kato H., Tanaka T., Nishioka T., Kimura A., Oda J. Role of cysteine residues in glutathione synthetase from Escherichia coli B. Chemical modification and oligonucleotide site-directed mutagenesis. J Biol Chem. 1988 Aug 25;263(24):11646–11651. [PubMed] [Google Scholar]
- Katre N. V. Immunogenicity of recombinant IL-2 modified by covalent attachment of polyethylene glycol. J Immunol. 1990 Jan 1;144(1):209–213. [PubMed] [Google Scholar]
- Katre N. V., Knauf M. J., Laird W. J. Chemical modification of recombinant interleukin 2 by polyethylene glycol increases its potency in the murine Meth A sarcoma model. Proc Natl Acad Sci U S A. 1987 Mar;84(6):1487–1491. doi: 10.1073/pnas.84.6.1487. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kimura A. Application of recDNA techniques to the production of ATP and glutathione by the "Syntechno System". Adv Biochem Eng Biotechnol. 1986;33:29–51. doi: 10.1007/BFb0002452. [DOI] [PubMed] [Google Scholar]
- Kondo T. [Glutathione metabolism in erythrocytes]. Tanpakushitsu Kakusan Koso. 1988 Jul;33(9):1466–1473. [PubMed] [Google Scholar]
- Konrad P. N., Valentine W. N., Paglia D. E. Enzymatic activities and glutathione content of erythrocytes in the newborn: comparison with red cells of older normal subjects and those with comparable reticulocytosis. Acta Haematol. 1972;48(4):193–201. doi: 10.1159/000208458. [DOI] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
- Landgraf B., Cohen F. E., Smith K. A., Gadski R., Ciardelli T. L. Structural significance of the C-terminal amphiphilic helix of interleukin-2. J Biol Chem. 1989 Jan 15;264(2):816–822. [PubMed] [Google Scholar]
- Meister A. Methods for the selective modification of glutathione metabolism and study of glutathione transport. Methods Enzymol. 1985;113:571–585. doi: 10.1016/s0076-6879(85)13077-6. [DOI] [PubMed] [Google Scholar]
- Niki E. [Scavenging of active oxygen by ascorbic acid and glutathione]. Tanpakushitsu Kakusan Koso. 1988 Dec;33(16):2973–2978. [PubMed] [Google Scholar]
- Sugi K., Inoue M., Morino Y. Degradation of plasma bilirubin by a bilirubin oxidase derivative which has a relatively long half-life in the circulation. Biochim Biophys Acta. 1989 Jun 27;991(3):405–409. doi: 10.1016/0304-4165(89)90065-2. [DOI] [PubMed] [Google Scholar]
- Takahashi K., Avissar N., Whitin J., Cohen H. Purification and characterization of human plasma glutathione peroxidase: a selenoglycoprotein distinct from the known cellular enzyme. Arch Biochem Biophys. 1987 Aug 1;256(2):677–686. doi: 10.1016/0003-9861(87)90624-2. [DOI] [PubMed] [Google Scholar]
- Takahashi K., Cohen H. J. Selenium-dependent glutathione peroxidase protein and activity: immunological investigations on cellular and plasma enzymes. Blood. 1986 Sep;68(3):640–645. [PubMed] [Google Scholar]
- Takakura Y., Fujita T., Hashida M., Maeda H., Sezaki H. Control of pharmaceutical properties of soybean trypsin inhibitor by conjugation with dextran. II: Biopharmaceutical and pharmacological properties. J Pharm Sci. 1989 Mar;78(3):219–222. doi: 10.1002/jps.2600780310. [DOI] [PubMed] [Google Scholar]
- Takakura Y., Kaneko Y., Fujita T., Hashida M., Maeda H., Sezaki H. Control of pharmaceutical properties of soybean trypsin inhibitor by conjugation with dextran. I: Synthesis and characterization. J Pharm Sci. 1989 Feb;78(2):117–121. doi: 10.1002/jps.2600780209. [DOI] [PubMed] [Google Scholar]
- Tietze F. Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues. Anal Biochem. 1969 Mar;27(3):502–522. doi: 10.1016/0003-2697(69)90064-5. [DOI] [PubMed] [Google Scholar]
- Tran L. T., Inoue Y., Kimura A. Oxidative stress response in yeast: purification and some properties of a membrane-bound glutathione peroxidase from Hansenula mrakii. Biochim Biophys Acta. 1993 Jul 10;1164(2):166–172. doi: 10.1016/0167-4838(93)90244-l. [DOI] [PubMed] [Google Scholar]
- Wada H., Imamura I., Sako M., Katagiri S., Tarui S., Nishimura H., Inada Y. Antitumor enzyme: polyethylene glycol-modified asparaginase. Ann N Y Acad Sci. 1990;613:95–108. doi: 10.1111/j.1749-6632.1990.tb18151.x. [DOI] [PubMed] [Google Scholar]
- Warso M. A., Lands W. E. Presence of lipid hydroperoxide in human plasma. J Clin Invest. 1985 Feb;75(2):667–671. doi: 10.1172/JCI111745. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Watanabe K., Yamano Y., Murata K., Kimura A. The nucleotide sequence of the gene for gamma-glutamylcysteine synthetase of Escherichia coli. Nucleic Acids Res. 1986 Jun 11;14(11):4393–4400. doi: 10.1093/nar/14.11.4393. [DOI] [PMC free article] [PubMed] [Google Scholar]
- White C. W., Jackson J. H., Abuchowski A., Kazo G. M., Mimmack R. F., Berger E. M., Freeman B. A., McCord J. M., Repine J. E. Polyethylene glycol-attached antioxidant enzymes decrease pulmonary oxygen toxicity in rats. J Appl Physiol (1985) 1989 Feb;66(2):584–590. doi: 10.1152/jappl.1989.66.2.584. [DOI] [PubMed] [Google Scholar]
- Yamaguchi H., Kato H., Hata Y., Nishioka T., Kimura A., Oda J., Katsube Y. Three-dimensional structure of the glutathione synthetase from Escherichia coli B at 2.0 A resolution. J Mol Biol. 1993 Feb 20;229(4):1083–1100. doi: 10.1006/jmbi.1993.1106. [DOI] [PubMed] [Google Scholar]
- Yasuda Y., Fujita T., Takakura Y., Hashida M., Sezaki H. Biochemical and biopharmaceutical properties of macromolecular conjugates of uricase with dextran and polyethylene glycol. Chem Pharm Bull (Tokyo) 1990 Jul;38(7):2053–2056. doi: 10.1248/cpb.38.2053. [DOI] [PubMed] [Google Scholar]
