Substrate-induced conformational changes in lactate dehydrogenase. Proteolysis of the immobilized enzyme in the presence of specific substrates.
Open Access
- 1 December 1977
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 252 (24), 8775-8777
- https://doi.org/10.1016/s0021-9258(17)38307-2
Abstract
No abstract availableThis publication has 10 references indexed in Scilit:
- Cross‐linking of reversibly immobilized enzymesFEBS Letters, 1977
- Evidence for the induction of a conformational change of trypsin by a specific substrate at pH 8.0Journal of Solid-Phase Biochemistry, 1976
- Evidence for the Induction of a Conformational Change of Bovine Trypsin by a Specific Substrate at pH 8.0Journal of Biological Chemistry, 1973
- Continuous spectrophotometric assay of a Sepharose-bound enzyme and its use to study kinetics of coupling of the enzyme to sepharoseAnalytical Biochemistry, 1973
- Structural Constraints of Possible Mechanisms of Lactate Dehydrogenase as Shown by High Resolution Studies of the Apoenzyme and a Variety of Enzyme ComplexesPublished by Cold Spring Harbor Laboratory ,1972
- The Action of Proteolytic Enzymes on N,N-Dimethyl ProteinsJournal of Biological Chemistry, 1969
- Complexes of chicken heart lactic dehydrogenase with coenzymes and substratesBiochemical and Biophysical Research Communications, 1968
- The effect of proteolysis and urea treatment on coenzyme binding to beef-heart lactic dehydrogenaseBiochimica et Biophysica Acta, 1961
- Fluorescence Studies of Coenzyme-binding to Beef Heart Lactic DehydrogenaseJournal of Biological Chemistry, 1959
- [67] Lactic dehydrogenase of muscleMethods in Enzymology, 1955