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PH-induced cold lability of rabbit skeletal muscle phosphofructokinase
Paul E. Bock,
Carl Frieden
Department of Biochemistry & Molecular Biophysics
Roy and Diana Vagelos Division of Biology & Biomedical Sciences (DBBS)
Institute of Clinical and Translational Sciences (ICTS)
Bursky Center for Human Immunology & Immunotherapy Programs (CHiiPs)
Research output
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Contribution to journal
›
Article
›
peer-review
41
Scopus citations
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Keyphrases
Active Enzyme
33%
ATP Binding
33%
Depolymerization
66%
Dissociation
33%
Enzyme Concentration
66%
Enzyme System
33%
Inactivation Mechanism
100%
Lability
100%
Light Scattering
33%
Low pH Value
33%
Low Temperature
33%
Molecular Events
33%
PH-induced
100%
Phosphate Buffer
33%
Phosphofructokinase
100%
Skeletal muscle
100%
Temperature Effect
33%
Biochemistry, Genetics and Molecular Biology
Adenosine Triphosphate
50%
Depolymerization
16%
Enzyme
100%
Leporidae
100%
Light Scattering
16%
Molecular Weight
16%
Phosphofructokinase
100%
Skeletal Muscle
100%
Engineering
Depolymerization
50%
Enzyme Concentration
100%
Function of Time
50%
Low-Temperature
50%
Molecular Mass
50%
Molecular Weight
50%
Process Result
100%
Earth and Planetary Sciences
Adenosine Triphosphate
100%
Depolymerization
33%
Light Scattering
33%
Molecular Weight
33%
Material Science
Adenosinetriphosphate
100%
Light Scattering
33%
Food Science
Light Scattering
100%