Abstract
To explore the secondary structures of lingual and pancreatic lipases, circular dichroism measurements were performed. Maximum average ellipticities were used to calculate the percentage of α-helices, β-sheets, and random coils. Lingual lipase had an ellipticity of −20235±140 deg cm 2/dmol(mean±SE) at 220nm suggesting 60% α-helix, 20% β-sheet and 20% random coil structure, but the mean ellipticity for pancreatic lipase was −14093±82 deg cm 2/dmol (mean ±SE) at 210nm suggesting a 34.8% α-helical, 25% β-sheet and 40% random coil secondary structure. An α-helical stretch of residues with a large hydrophobic moment (“globular” α-helix by hydrophobic moment plot) from amino acids 382 through 389 at the COOH-terminal end of lingual lipase was noted. This sequence, absent in pancreatic lipase, may account for the avid binding of lingual lipase to fat emulsion particles.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Biochemical and Biophysical Research Communications
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
