Hydrolysis of fluorescent pyrene-acyl esters by human pancreatic carboxylic ester hydrolase and bile salt-stimulated lipase

Lipids ◽  
1990 ◽  
Vol 25 (8) ◽  
pp. 428-434 ◽  
Author(s):  
Anne Negre-Salvayre ◽  
Nehza Abouakil ◽  
Dominique Lombardo ◽  
Robert Salvayre
1983 ◽  
Vol 133 (2) ◽  
pp. 327-333 ◽  
Author(s):  
Dominique LOMBARDO ◽  
Daniel CAMPESE ◽  
Luc MULTIGNER ◽  
Huguette LAFONT ◽  
Alain CARO

1990 ◽  
Vol 192 (2) ◽  
pp. 543-550 ◽  
Author(s):  
Jeanette NILSSON ◽  
Lars BLACKBERG ◽  
Peter CARLSSON ◽  
Seven ENERBACK ◽  
Olle HERNELL ◽  
...  

2000 ◽  
Vol 267 (8) ◽  
pp. 2227-2234 ◽  
Author(s):  
Sylvie Smialowski-Fléter ◽  
André Moulin ◽  
Claude Villard ◽  
Antoine Puigserver

1978 ◽  
Vol 24 (7) ◽  
pp. 1177-1181 ◽  
Author(s):  
W K Lam ◽  
E Taft ◽  
L T Yam

Abstract A carboxylic-ester hydrolase was isolated from the leukocytes of a patient with myelomonocytic leukemia. Its relative molecular mass as estimated by sucrose density-gradient sedimentation is about 70 000. The purified enzyme is specific for acetyl esters of aromatic alcohols. It is inhibited by fluoride, but insensitive to eserine or p-chloromercuriphenylsulfonate. Hydrolysis of 1-naphthyl acetate was optimal above pH 6.0; of o-nitrophenyl acetate, above 8.0. The common catalytic site for the two types of substrates on the enzyme was confirmed by competitive inhibition data.


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