EFFECTS OF LIGAND-BINDING AND SUBUNIT ASSOCIATION ON THE HYDROGEN-EXCHANGE KINETICS OF ESCHERICHIA-COLI ASPARTATE-TRANSCARBAMYLASE

被引：0

作者：

LENNICK, M ^{[1
]}

ALLEWELL, NM ^{[1
]}

机构：

[1] WESLEYAN UNIV,MIDDLETOWN,CT 06457

来源：

BIOPHYSICAL JOURNAL | 1981年 / 33卷 / 02期

关键词：

D O I：

暂无

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

引用

页码：A138 / A138

页数：1

共 50 条

[41] PH-DEPENDENCE OF THERMODYNAMIC PARAMETERS FOR BINDING OF SUBSTRATE ANALOGS TO ESCHERICHIA-COLI ASPARTATE-TRANSCARBAMYLASE
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HOFMANN, G
ZAUG, A
BIOPHYSICAL JOURNAL, 1978, 21 (03) : A138 - A138
[42] ORDERED SUBSTRATE BINDING AND EVIDENCE FOR A THERMALLY INDUCED CHANGE IN MECHANISM FOR ESCHERICHIA-COLI ASPARTATE-TRANSCARBAMYLASE
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[43] SUBUNIT INTERACTIONS IN ASPARTATE-TRANSCARBAMYLASE FROM ESCHERICHIA-COLI STUDIED USING MATRIX-BOUND DERIVATIVES
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[44] EFFECT OF ENZYME AND LIGAND CONCENTRATION ON STATE OF AGGREGATION OF ASPARTATE-TRANSCARBAMYLASE OF ESCHERICHIA-COLI .1. BINDING OF CTP AND ATP TO ENZYME
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[45] BOHR EFFECT IN ESCHERICHIA-COLI ASPARTATE-TRANSCARBAMYLASE - LINKAGES BETWEEN SUBSTRATE BINDING, PROTON BINDING, AND CONFORMATIONAL TRANSITIONS
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[46] COMPARISON OF VANTHOFF AND CALORIMETRICALLY DETERMINED ENTHALPIES OF BINDING OF N-PHOSPHONACETYL-L-ASPARTATE TO ESCHERICHIA-COLI ASPARTATE-TRANSCARBAMYLASE
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KNIER, BL
ALLEWELL, NM
BIOPHYSICAL CHEMISTRY, 1979, 10 (01) : 47 - 54
[47] STRUCTURAL CONSEQUENCES OF A ONE ATOM MUTATION ON ASPARTATE-TRANSCARBAMYLASE FROM ESCHERICHIA-COLI
CHERFILS, J
SWEET, RM
MIDDLETON, SA
KANTROWITZ, ER
TAUC, P
VACHETTE, P
FEBS LETTERS, 1989, 247 (02) : 361 - 366
[48] ESCHERICHIA-COLI ASPARTATE-TRANSCARBAMYLASE INVESTIGATED BY TRANSVERSE UREA GEL-ELECTROPHORESIS
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GIANGRANDE, PH
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[49] 3 RESIDUES INVOLVED IN BINDING AND CATALYSIS IN THE CARBAMYL-PHOSPHATE BINDING-SITE OF ESCHERICHIA-COLI ASPARTATE-TRANSCARBAMYLASE
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XU, W
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[50] THERMODYNAMIC AND KINETIC LINKAGES BETWEEN LIGAND-BINDING, FOLDING AND ASSEMBLY OF THE CATALYTIC SUBUNIT OF ESCHERICHIA-COLI ASPARTATE TRANSCARBAMOYLASE
BROMBERG, S
ALLEWELL, N
BIOPHYSICAL JOURNAL, 1988, 53 (02) : A451 - A451

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