Superoxide dismutase activity of a Cu-Zn complex -: bare and immobilised

被引:28
|
作者
Szilágyi, I
Labádi, I
Hernadi, K
Pálinkó, I
Fekete, I
Korecz, L
Rockenbauer, A
Kiss, T
机构
[1] Univ Szeged, Dept Organ Chem, H-6720 Szeged, Hungary
[2] Univ Szeged, Dept Inorgan & Analyt Chem, H-6720 Szeged, Hungary
[3] Univ Szeged, Dept Organ Chem, H-6720 Szeged, Hungary
[4] Univ Szeged, Dept Phys Geog & Geoinformat, H-6720 Szeged, Hungary
[5] Inst Struct Chem, Chem Res Ctr, H-1525 Budapest, Hungary
[6] Univ Szeged, Hungarian Acad Sci, Bioinorgan Chem Res Grp, H-6720 Szeged, Hungary
关键词
D O I
10.1039/b500579e
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
A binuclear, imidazolato-bridged complex (Cu(II)-diethylenetriamino-mu-imidazolato-Zn(II)-tris(aminoethyl)amine perchlorate) was prepared and immobilised on silica gel or among the layers of montmorillonite. Immobilisation occurred via hydrogen bonding for the silica gel and through electrostatic forces for the montmorillonite. The obtained substances were characterised by EPR and FT-IR spectroscopies and their thermal behaviour was studied by thermogravimetry. The superoxide dismutase ( SOD) activity of the complex before and after immobilisation was studied by a SOD assay. It was found that the SOD activity of the host-free complex increased by more than an order of magnitude and approached the efficiency of the real enzyme when silica gel was used as host. The enhanced activity could be assigned to the formation of magnetically isolated centers in the silica pores. On the other hand, the immobilisation with montmorillonite slightly reduced the SOD activity.
引用
收藏
页码:740 / 745
页数:6
相关论文
共 50 条
  • [1] SEMIAUTOMATED ASSAY OF ERYTHROCYTE CU-ZN SUPEROXIDE-DISMUTASE ACTIVITY
    FULBERT, JC
    SUCCARI, M
    CALS, MJ
    CLINICAL BIOCHEMISTRY, 1992, 25 (02) : 115 - 119
  • [2] BIOPHYSICAL STUDIES OF CU-ZN SUPEROXIDE-DISMUTASE
    BUTLER, A
    PEOPLES, RJ
    AVDEEF, A
    VALENTINE, JS
    BIOPHYSICAL JOURNAL, 1983, 41 (02) : A272 - A272
  • [3] Studies on simulation chemistry of Cu-Zn superoxide dismutase
    Luo, QH
    CHEMICAL JOURNAL OF CHINESE UNIVERSITIES-CHINESE, 1997, 18 (07): : 1012 - 1018
  • [4] THE SEQUENCE OF THE CU-ZN SUPEROXIDE-DISMUTASE GENE OF DROSOPHILA
    SETO, NOL
    HAYASHI, S
    TENER, GM
    NUCLEIC ACIDS RESEARCH, 1987, 15 (24) : 10601 - 10601
  • [5] DROSOPHILA CU-ZN SUPEROXIDE-DISMUTASE CDNA SEQUENCE
    SETO, NOL
    HAYASHI, S
    TENER, GM
    NUCLEIC ACIDS RESEARCH, 1987, 15 (13) : 5483 - 5483
  • [6] Purification and properties of Oryza sativa Cu-Zn superoxide dismutase
    Padiglia, A
    Medda, R
    Cruciani, E
    Lorrai, A
    Floris, G
    PREPARATIVE BIOCHEMISTRY & BIOTECHNOLOGY, 1996, 26 (02): : 135 - 142
  • [7] THE PRIMARY STRUCTURE OF CU-ZN SUPEROXIDE-DISMUTASE FROM PHOTOBACTERIUM-LEIOGNATHI - EVIDENCE FOR A SEPARATE EVOLUTION OF CU-ZN SUPEROXIDE-DISMUTASE IN BACTERIA
    STEFFENS, GJ
    BANNISTER, JV
    BANNISTER, WH
    FLOHE, L
    GUNZLER, WA
    KIM, SMA
    OTTING, F
    HOPPE-SEYLERS ZEITSCHRIFT FUR PHYSIOLOGISCHE CHEMIE, 1983, 364 (06): : 675 - 690
  • [8] In Silico Analysis of Cu-Zn Superoxide Dismutase and Mn Superoxide Dismutase Genes in Fugu (Takifugu rubripes)
    Bayir, Mehtap
    PAKISTAN JOURNAL OF ZOOLOGY, 2020, 52 (04) : 1377 - 1382
  • [9] CLONING, EXPRESSION, AND OCCURRENCE OF THE BRUCELLA CU-ZN SUPEROXIDE-DISMUTASE
    BRICKER, BJ
    TABATABAI, LB
    JUDGE, BA
    DEYOE, BL
    MAYFIELD, JE
    INFECTION AND IMMUNITY, 1990, 58 (09) : 2935 - 2939
  • [10] Inhibition of yeast ribosomal stalk phosphorylation by Cu-Zn superoxide dismutase
    Zielinski, R
    Pilecki, M
    Kubinski, K
    Zien, P
    Hellman, U
    Szyszka, R
    BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2002, 296 (05) : 1310 - 1316