The diverse Michaelis constants and maximum velocities of lactate dehydrogenase in situ in various types of cell
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Anatomy
Link
http://link.springer.com/content/pdf/10.1007/BF00157761.pdf
Reference29 articles.
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2. Battellino, L. J., Jaime, F. R. & Blanco, A. (1968) Kinetic properties of rabbit testicular lactate dehydrogenase isozyme. J. Biol. Chem. 243, 5185?92.
3. Bennett, N. G. & Gutfreund, H. (1973) The kinetics of the interconversion of intermediates of the reaction of pig muscle lactate dehydrogenase with oxidized nicotinamideadenine dinucleotide and lactate. Biochem. J. 135, 81?5.
4. Butcher, R. G. (1978) The measurement in tissue sections of the two formazans derived from Nitroblue Tetrazolium in dehydrogenase reactions. Histochem. J. 10, 739?44.
5. Costello, L. A. & Kaplan, N. O. (1963) Evidence for two forms of M-type lactate dehydrogenase in the mouse. Biochim. Biophys. Acta 73, 658?60.
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