Temperature adaptation of enzymes: roles of the free energy, the enthalpy, and the entropy of activation

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Temperature adaptation of enzymes: roles of the free energy, the enthalpy, and the entropy of activation is …
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scholarly articleQ13442814

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P819ADS bibcode1973PNAS...70..430L
P356DOI10.1073/PNAS.70.2.430
P932PMC publication ID433275
P698PubMed publication ID4510286
P5875ResearchGate publication ID18656349

P50authorPhilip S. LowQ40021294
George N. SomeroQ87855106
P2093author name stringBada JL
P2860cites workStructural and Catalytic Properties of Lobster Muscle Glycogen PhosphorylaseQ93792563
The Catalytic and Regulatory Properties of EnzymesQ39974037
Structure and Catalytic Activity of Alcohol DehydrogenasesQ58953184
Glyceraldehyde 3-Phosphate Dehydrogenase from Pig MuscleQ59056349
Structural and functional properties of the H and M subunits of lactic dehydrogenasesQ70874241
Conformational changes in rabbit muscle aldolase. Kinetic studiesQ71545041
Comparative studies on the activity of d-glyceraldehyde-3-phosphate dehyrogenase from cold and warm-blooded animals with reference to temperatureQ72367374
The comparative enzymology of lactic dehydrogenases. IV. Function of sulfhydryl groups in lactic dehydrogenases and the sequence around the essential groupQ72599909
P433issue2
P407language of work or nameEnglishQ1860
P921main subjectenthalpyQ161064
P304page(s)430-432
P577publication date1973-02-01
P1433published inProceedings of the National Academy of Sciences of the United States of AmericaQ1146531
P1476titleTemperature adaptation of enzymes: roles of the free energy, the enthalpy, and the entropy of activation
P478volume70

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