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Cited by 345

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Inhibition of pancreatic lipase in vitro by the covalent inhibitor tetrahydrolipstatin

Open access
Hadváry, P, Lengsfeld, H, Wolfer, H·1988·Biochemical Journal

Abstract

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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Crossref · 10.1042/bj2560357

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Metadata

Authors
Hadváry, P., Lengsfeld, H., & Wolfer, H.
Venue
Biochemical Journal
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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CoChat. (2026). Citation check: Inhibition of pancreatic lipase in vitro by the covalent inhibitor tetrahydrolipstatin. https://app.cochat.ai/papers/10.1042/bj2560357
The paper
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).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.