Document Detail


Biochemical characterization, cloning, and molecular modelling of chicken pancreatic lipase.
MedLine Citation:
PMID:  16780787     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Chicken pancreatic lipase (CPL) was purified from delipidated pancreas. Pure CPL was obtained after ammonium sulphate fractionation, then DEAE-cellulose, Sephacryl S-200 gel filtration, and FPLC Mono-Q Sepharose columns. The pure lipase is a glycosylated monomer having a molecular mass of about 50kDa. The 23 N-terminal amino acid residues of CPL were sequenced. The sequence is similar to those of avian and mammalian pancreatic lipases. CPL presents the interfacial activation phenomenon tested with tripropionin or vinyl ester. When CPL was inhibited by synthetic detergent (TX-100) or amphipathic protein (BSA), simultaneous addition of bile salts and colipase was required to restore the full CPL activity. In the absence of colipase and bile salts, CPL was unable to hydrolyse tributyrin emulsion. This enzyme can tolerate, more efficiently than HPL, the accumulation of long-chain free fatty acids at the interface when olive oil emulsion was used as substrate in the absence of bile salts and colipase. The CPL activity, under these conditions, was linear whereas that of HPL decreased rapidly. Anti-TPL polyclonal antibodies cross-reacted specifically with CPL. The gene encoding the mature CPL was cloned and sequenced. The deduced amino acid sequence of the mature lipase shows a high degree of homology with the mammalian pancreatic lipases. A 3D structure model of CPL was built using the HPL structure as template. We have concluded that a slight increase in the exposed hydrophobic residues on the surface of CPL, as compared to HPL, could be responsible for a higher tolerance to the presence of long-chain free fatty acids at the lipid/water interface.
Authors:
Ahmed Fendri; Fakher Frikha; Habib Mosbah; Nabil Miled; Nacim Zouari; Abir Ben Bacha; Adel Sayari; Hafedh Mejdoub; Youssef Gargouri
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Publication Detail:
Type:  Comparative Study; Journal Article     Date:  2006-05-17
Journal Detail:
Title:  Archives of biochemistry and biophysics     Volume:  451     ISSN:  0003-9861     ISO Abbreviation:  Arch. Biochem. Biophys.     Publication Date:  2006 Jul 
Date Detail:
Created Date:  2006-07-14     Completed Date:  2006-08-21     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0372430     Medline TA:  Arch Biochem Biophys     Country:  United States    
Other Details:
Languages:  eng     Pagination:  149-59     Citation Subset:  IM    
Affiliation:
Laboratoire de Biochimie et de Génie Enzymatique des Lipases, ENIS, BPW, Sfax 3038, Tunisia.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Base Sequence
Bile Acids and Salts / pharmacology
Chickens
Cloning, Molecular*
Colipases / pharmacology
Detergents / pharmacology
Emulsions / metabolism
Humans
Hydrophobicity
Lipase / chemistry*,  genetics*,  isolation & purification,  metabolism
Models, Molecular*
Molecular Sequence Data
Molecular Weight
Octoxynol / pharmacology
Pancreas / enzymology*
Plant Oils / pharmacology
Sequence Analysis, Protein
Triglycerides / metabolism,  pharmacology
Chemical
Reg. No./Substance:
0/Bile Acids and Salts; 0/Colipases; 0/Detergents; 0/Emulsions; 0/Plant Oils; 0/Triglycerides; 139-45-7/tripropionin; 60-01-5/tributyrin; 8001-25-0/olive oil; 9002-93-1/Octoxynol; EC 3.1.1.3/Lipase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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