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Inhibition of pancreatic lipase in vitro by the covalent inhibitor tetrahydrolipstatin
Open accessAbstract
Tetrahydrolipstatin inhibits pancreatic lipase from several species, including man, with comparable potency. The lipase is progressively inactivated through the formation of a long-lived covalent intermediate, probably with a 1:1 stoichiometry. The lipase substrate triolein and also a boronic acid derivative, which is presumed to be a transition-state-form inhibitor, retard the rate of inactivation. Therefore, in all probability, tetrahydrolipstatin reacts with pancreatic lipase at, or near, the substrate binding or active site. Tetrahydrolipstatin is a selective inhibitor of lipase; other hydrolases tested were at least a thousand times less potently inhibited.
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Cites
A RAPID METHOD OF TOTAL LIPID EXTRACTION AND PURIFICATION
Bligh, E. G., & Dyer, W. J. (1959) · Canadian Journal of Biochemistry and Physiology · doi:10.1139/o59-099 · Cited by 54,751
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Klein, S., Burke, L. E., Bray, G. A., Blair, S., Allison, D. B., Pi-Sunyer, X., Hong, Y., & Eckel, R. H. (2004) · Circulation · doi:10.1161/01.cir.0000145546.97738.1e · Cited by 934
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Hadváry, P., Sidler, W., Meister, W., Vetter, W., & Wolfer, H. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)52203-1 · Cited by 280
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Metadata
- Authors
- Hadváry, P., Lengsfeld, H., & Wolfer, H.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1988-12-01
- Volume
- 256
- Issue
- 2
- Pages
- 357-361
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W1939955036
- Cited by
- 345
- References
- 1
- FWCI
- 1.40
- Type
- journal article
- Language
- en
- Open access
- green
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- Hadváry, P., Lengsfeld, H., & Wolfer, H. (1988). Inhibition of pancreatic lipase in vitro by the covalent inhibitor tetrahydrolipstatin. Biochemical Journal. https://doi.org/10.1042/bj2560357
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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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