The lipase inhibitor tetrahydrolipstatin binds covalently to the putative active site serine of pancreatic lipase
Open Access
- 1 February 1991
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 266 (4) , 2021-2027
- https://doi.org/10.1016/s0021-9258(18)52203-1
Abstract
No abstract availableKeywords
This publication has 22 references indexed in Scilit:
- Tetrahydrolipstatin: Thermal and Hydrolytic DegradationHelvetica Chimica Acta, 1990
- Charge-remote fragmentations of closed-shell ions. A thermolytic analogyJournal of the American Chemical Society, 1989
- Mode of action of tetrahydrolipstatin: a derivative of the naturally occurring lipase inhibitor lipstatinBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1988
- Contributions of mass spectrometry to peptide and protein structureJournal of Mass Spectrometry, 1988
- Syntheses of Tetrahydrolipstatin and Absolute Configuration of Tetrahydrolipstatin and LipstatinHelvetica Chimica Acta, 1987
- Which class of serine is involved in the lipase mechanism?Trends in Biochemical Sciences, 1986
- Hydrolysis of p‐nitrophenyl acetate by the peptide chain fragment (336–449) of porcine pancreatic lipaseEuropean Journal of Biochemistry, 1986
- Mechanism of pancreatic lipase action. 2. Catalytic properties of modified lipasesBiochemistry, 1976
- The Complete Amino Acid Sequences of Both Subunits of the Sweet Protein MonellinHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1976
- Charge participation in the fragmentation of functionalized steroidsJournal of Mass Spectrometry, 1970