STRUCTURAL-CHANGES IN CELLOBIOHYDROLASE I UPON BINDING OF A MACROMOLECULAR LIGAND AS EVIDENT BY SAXS INVESTIGATIONS

被引：15
作者：
ABUJA, PM
PILZ, I
TOMME, P
CLAEYSSENS, M
机构：
[1] GRAZ UNIV, INST PHYS CHEM, HEINRICHSTR 28, A-8010 GRAZ, AUSTRIA
[2] STATE UNIV GHENT, BIOCHEM LAB, B-9000 GHENT, BELGIUM
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1989年 / 165卷 / 02期
关键词：
D O I：
10.1016/S0006-291X(89)80010-5
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
引用
收藏
页码：615 / 623
页数：9
相关论文
共 11 条
  • [1] ABUJA PM, 1988, EUR BIOPHYS J BIOPHY, V15, P339, DOI 10.1007/BF00254721
  • [2] DOMAIN-STRUCTURE OF CELLOBIOHYDROLASE-II AS STUDIED BY SMALL-ANGLE X-RAY-SCATTERING - CLOSE RESEMBLANCE TO CELLOBIOHYDROLASE-I
    ABUJA, PM
    PILZ, I
    CLAEYSSENS, M
    TOMME, P
    [J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1988, 156 (01) : 180 - 185
  • [3] NEW METHOD FOR EVALUATION OF SMALL-ANGLE SCATTERING DATA
    GLATTER, O
    [J]. JOURNAL OF APPLIED CRYSTALLOGRAPHY, 1977, 10 (OCT1) : 415 - 421
  • [4] GLATTER O, 1980, ACTA PHYS AUSTRIACA, V52, P243
  • [5] Glatter O., 1982, SMALL ANGLE XRAY SCA
  • [6] MONTENECOURT BS, 1979, FEBS LETT, V2, P239
  • [7] Pilz I, 1979, Methods Enzymol, V61, P148
  • [8] STUDIES OF THE CELLULOLYTIC SYSTEM OF TRICHODERMA-REESEI QM-9414 - ANALYSIS OF DOMAIN FUNCTION IN 2 CELLOBIOHYDROLASES BY LIMITED PROTEOLYSIS
    TOMME, P
    VANTILBEURGH, H
    PETTERSSON, G
    VANDAMME, J
    VANDEKERCKHOVE, J
    KNOWLES, J
    TEERI, T
    CLAEYSSENS, M
    [J]. EUROPEAN JOURNAL OF BIOCHEMISTRY, 1988, 170 (03): : 575 - 581
  • [9] IDENTIFICATION OF A FUNCTIONALLY IMPORTANT CARBOXYL GROUP IN CELLOBIOHYDROLASE-I FROM TRICHODERMA-REESEI - A CHEMICAL MODIFICATION STUDY
    TOMME, P
    CLAEYSSENS, M
    [J]. FEBS LETTERS, 1989, 243 (02): : 239 - 243
  • [10] LIMITED PROTEOLYSIS OF THE CELLOBIOHYDROLASE I FROM TRICHODERMA-REESEI - SEPARATION OF FUNCTIONAL DOMAINS
    VANTILBEURGH, H
    TOMME, P
    CLAEYSSENS, M
    BHIKHABHAI, R
    PETTERSSON, G
    [J]. FEBS LETTERS, 1986, 204 (02) : 223 - 227
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