Catalytic efficiency and structural properties of invertebrate muscle pyruvate kinases: Correlation with body temperature and oxygen consumption rates

Author:

Hoffmann Klaus-Hubert

Publisher

Springer Science and Business Media LLC

Subject

Endocrinology,Animal Science and Zoology,Biochemistry,Ecology, Evolution, Behavior and Systematics,Physiology,General Earth and Planetary Sciences,General Environmental Science

Reference26 articles.

1. Altman, P.L., Dittmer, D.S.: Metabolism. Bethesda: Federation of American Societies for Experimental Biology 1968

2. Alexandrov, V.Y.: Conformational flexibility of proteins and their resistance to proteinases and temperature conditions of life. Curr. Mod. Biol.3, 9?19 (1969)

3. Baily, E., Stirpe, F., Taylor, C.B.: Regulation of rat liver pyruvate kinase. Biochem. J.108, 427?436 (1968)

4. Baldwin, J.: Selection for catalytic efficiency of lactate dehydrogenase M4: Correlation with body temperature and levels of anaerobic glycolysis. Comp. Biochem. Physiol.52B, 33?37 (1975)

5. Berkel, J.C. van, Koster, J.F., Hülsmann, W.C.: Two interconvertible forms of L-Type pyruvate kinase from rat liver. Biochim. biophys. Acta (Amst.)293, 118?124 (1973)

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