ADENOSINE CYCLIC 3',5'-MONOPHOSPHATE DEPENDENT PROTEIN-KINASE - A NEW FLUORESCENCE DISPLACEMENT TITRATION TECHNIQUE FOR CHARACTERIZING THE NUCLEOTIDE BINDING-SITE ON THE CATALYTIC SUBUNIT

被引：80

作者：

BHATNAGAR, D

ROSKOSKI, R

ROSENDAHL, MS

LEONARD, NJ

机构：

[1] LOUISIANA STATE UNIV,MED CTR,DEPT BIOCHEM,NEW ORLEANS,LA 70119

[2] UNIV ILLINOIS,DEPT MED,URBANA,IL 61801

[3] UNIV ILLINOIS,DEPT BIOCHEM,URBANA,IL 61801

来源：

BIOCHEMISTRY | 1983年 / 22卷 / 26期

关键词：

D O I：

10.1021/bi00295a042

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

页码：6310 / 6317

页数：8

共 49 条

[1] MAGNETIC-RESONANCE AND KINETIC STUDIES OF THE MANGANESE(II) ION AND SUBSTRATE COMPLEXES OF THE CATALYTIC SUBUNIT OF ADENOSINE-3',5'-MONOPHOSPHATE DEPENDENT PROTEIN-KINASE FROM BOVINE HEART
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[2] CYCLIC AMP-DEPENDENT ATPASE ACTIVITY OF BOVINE HEART PROTEIN-KINASE
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[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1979, 76 (02) : 722 - 725
[3] Beavo J A, 1975, Adv Cyclic Nucleotide Res, V5, P241
[4] STRUCTURE OF HORSE MUSCLE PHOSPHOGLYCERATE KINASE - SOME RESULTS ON CHAIN CONFORMATION, SUBSTRATE BINDING AND EVOLUTION OF MOLECULE FROMA 3 A FOURIER MAP
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EVANS, PR
[J]. JOURNAL OF MOLECULAR BIOLOGY, 1974, 84 (04) : 585 - 601
[5] STEREOCHEMICAL AND KINETIC-STUDIES ON THE ACTION OF THE CATALYTIC SUBUNIT OF BOVINE CARDIAC-MUSCLE ADENOSINE-3',5'-MONOPHOSPHATE DEPENDENT PROTEIN-KINASE USING METAL-ION COMPLEXES OF ATP-BETA-S
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KAISER, ET
[J]. BIOCHEMISTRY, 1980, 19 (06) : 1176 - 1182
[6] ADENOSINE CYCLIC 3',5'-MONOPHOSPHATE DEPENDENT PROTEIN-KINASE - KINETIC MECHANISM FOR THE BOVINE SKELETAL-MUSCLE CATALYTIC SUBUNIT
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HARTL, FT
ROSKOSKI, R
[J]. BIOCHEMISTRY, 1982, 21 (23) : 5794 - 5799
[7] CORBIN JD, 1975, J BIOL CHEM, V250, P218
[8] CORBIN JD, 1981, PROTEIN PHOSPHORYLAT, V8, P45
[9] ISOLATION AND PROPERTIES OF RABBIT SKELETAL-MUSCLE PROTEIN INHIBITOR OF ADENOSINE-3',5'-MONOPHOSPHATE DEPENDENT PROTEIN-KINASES
DEMAILLE, JG
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[J]. BIOCHEMISTRY, 1977, 16 (14) : 3080 - 3086
[10] ERLICHMAN J, 1974, J BIOL CHEM, V249, P5000

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