Document Detail

The environment of tryptophan in pig pancreatic phospholipase A2 bound to bilayers.
MedLine Citation:
PMID:  3978097     Owner:  NLM     Status:  MEDLINE    
Binding of pig pancreatic phospholipase A2 to ternary codispersions of diacylphosphatidylcholine/lysophosphatidylcholine/fatty acid (100:22:22, mole ratio) is monitored by the increase in intrinsic fluorescence intensity of the single tryptophan residue. The fluorescence is quenched by the brominated fatty acid components in the ternary codispersions. The quenching efficiency is in the order: 11,12-dibromo- greater than 9,10-dibromo- greater than 6,7-dibromo- greater than 2-bromo fatty acid. The quenching efficiency of the 9,10-brominated derivatives of the three components in the ternary codispersions is in the order diacylphosphatidylcholine greater than fatty acid greater than lysophosphatidylcholine. Two isomers of diacylphosphatidylcholine with 9,10-dibromo substituents on chain 1 or 2 are equally efficient quenchers. While succinimide also quenches the fluorescence of the free and the membrane bound enzyme, the tryptophan residue in both systems is not accessible to 1-methylnicotinamide. These results are rationalized by a hypothesis that the acyl chains of the substrate interacts with the tryptophan residue of pig pancreatic phospholipase A2, which is readily accessible to water soluble neutral quenchers both in the free and the bound state.
M K Jain; B P Maliwal
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  814     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1985 Mar 
Date Detail:
Created Date:  1985-05-20     Completed Date:  1985-05-20     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  135-40     Citation Subset:  IM    
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MeSH Terms
Lipid Bilayers / metabolism*
Pancreas / enzymology*
Phospholipases / metabolism*
Phospholipases A / metabolism*
Phospholipases A2
Grant Support
Reg. No./Substance:
0/Lipid Bilayers; 73-22-3/Tryptophan; EC 3.1.-/Phospholipases; EC 3.1.1.-/Phospholipases A; EC A2

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