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Action of Phospholipase A at Interfaces
Open accessAbstract
Abstract The heterogeneous catalysis of pancreatic phospholipase A (EC 3.1.1.4) is studied by kinetics on monomolecular layers of short chain phospholipids. Under certain conditions long induction times are observed experimentally which can be related with a slow reversible penetration of the enzyme into the monolayer. The influence of surface pressure, pH, sodium chloride, and Ca2+ ions on this penetration step is reported. Based on a proposed two-dimensional Michaelis model, steady state and presteady state equations are derived and together with computer analysis show a good fit with the experimental results. A quantitative comparison between enzyme kinetics obtained by monolayer and bulk techniques is attempted using a common definition of the quality of the lipid-water interface. Possible implications of the concept of a penetration site on the enzyme are discussed.
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Cited by
Kinetics of the activation of plasminogen by human tissue plasminogen activator. Role of fibrin.
Hoylaerts, M., Rijken, D. C., Lijnen, H. R., & Collen, D. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)81051-7 · Cited by 1,312
Enzymatic Reactions in Giant Vesicles
Walde, P. (1999) · Perspectives in Supramolecular Chemistry · doi:10.1002/9780470511534.ch22 · Cited by 2
Metadata
- Authors
- Verger, R., Mieras, M. C. E., & de Haas, G. H.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1973-06
- Volume
- 248
- Issue
- 11
- Pages
- 4023-4034
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1533793715
- Cited by
- 507
- References
- 0
- FWCI
- 6.53
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Verger, R., Mieras, M. C. E., & de Haas, G. H. (1973). Action of Phospholipase A at Interfaces. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)43833-7
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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