Microheterogeneity of enzymes and deactivation
- 20 December 1987
- journal article
- research article
- Published by Wiley in Biotechnology & Bioengineering
- Vol. 30 (9) , 1041-1056
- https://doi.org/10.1002/bit.260300907
Abstract
The influence of microheterogeneity on enzyme inactivation kinetics is presented. Examples of different enzymes are given where microheterogeneity has been detected by different techniques. The different statistical models are presented which include the influence of microheterogeneity on enzyme inactivation kinetics and stability. As the microheterogeneity of the enzyme increases, there is a sharper decline in the normalized activity during the initial stages of the deactivation but a greater stability and activity, compared to similar homogeneous enzyme, as the deactivation proceeds. Microheterogeneity makes the deactivation reaction have a higher apparent order of reaction. The implications of microheterogeneity on enzyme inactivations are high lighted by different examples. The analysis provides fresh physical insights into the chemistry, subpopulations, structure, and function of enzymes.Keywords
This publication has 54 references indexed in Scilit:
- Theory of sedimentation for antigen-antibody reactions: Effect of antibody heterogeneity on the shape of the patternMolecular Immunology, 1982
- Plasma High-Density LipoproteinsNew England Journal of Medicine, 1978
- Microheterogeneity of plasma albumins. V. Permutations in disulfide pairings as a probable source of microheterogeneity in bovine albuminBiochemistry, 1969
- Electrophoretic Behavior of Bovine Plasma Albumin At Low pHJournal of the American Chemical Society, 1957
- Ultracentrifugal Properties of Human γ-Globulins Prepared by Electrophoresis—Convection1,2Journal of the American Chemical Society, 1953
- Boundary Spreading in Sedimentation Velocity Experiments. I. The Enzymatic Degradation of Serum GlobulinsJournal of the American Chemical Society, 1952
- Isolation of an Electrophoretically Homogeneous Crystalline Component of β-Lactoglobulin2Journal of the American Chemical Society, 1950
- Preparation of Cytochrome c with the Aid of Ion Exchange Resin.Acta Chemica Scandinavica, 1950
- A Quantitative Study of Reversible Boundary Spreading in the Electrophoresis of Proteins1Journal of the American Chemical Society, 1948
- The Serological Properties of Simple Substances. VII. A Quantitative Theory of the Inhibition by Haptens of the Precipitation of Heterogeneous Antisera with Antigens, and Comparison with Experimental Results for Polyhaptenic Simple Substances and for AzoproteinsJournal of the American Chemical Society, 1944