Properties of lactate dehydrogenase crystals reacted with diimidoesters
Author:
Publisher
Springer Science and Business Media LLC
Subject
Biochemistry,General Medicine
Link
http://link.springer.com/content/pdf/10.1007/BF02906282.pdf
Reference19 articles.
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2. Bloxham, D. P. &D. C. Wilton: Modification of pig heart lactate dehydrogenase with methyl methanethiouslphonate to produce an enzyme with altered catalytic activity. Biochem. J. 161, 643–651 (1977)
3. Boland, M. J. &H. Gutfreund: Pig heart lactate dehydrogenase. Binding of pyruvate and the interconversion of pyruvate-containing ternary complexes. Biochem. J. 161, 715–727 (1975)
4. Cornish-Bowden, A.: Principles of enzyme kinetics. Butterworths London, pp. 168–193 (1976)
5. Dalziel, K.: Initial steady state velocities in the evaluation of enzyme-coenzyme-substrate reaction mechanisms. Acta Chem. Scand. 11, 1706–1723 (1957)
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1. References;Bioconjugate Techniques;2008
2. Cross-Linked LDH Crystals for Lactate Synthesis Coupled to Electroenzymatic Regeneration of NADH;The Journal of Organic Chemistry;1996-01-01
3. References;Bioconjugate Techniques;1996
4. Enzymes immobilized as crystals. Hydrogen isotope exchange of crystalline lysozyme;Biochimie;1980-09
5. Buoyant densities of dissolved and crystalline lactate dehydrogenase from pig heart and pig muscle;Carlsberg Research Communications;1978-11
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