Spectrofluorimetric study of the bile salt micelle binding site of pig and horse colipases

Author(s):  
S. Granon
2011 ◽  
Vol 80 (3) ◽  
pp. 935-945 ◽  
Author(s):  
Michael L. Barta ◽  
Manita Guragain ◽  
Philip Adam ◽  
Nicholas E. Dickenson ◽  
Mrinalini Patil ◽  
...  

1975 ◽  
Vol 65 (2) ◽  
pp. 740-745 ◽  
Author(s):  
M. Charles ◽  
H. Sari ◽  
B. Entressangles ◽  
P. Desnuelle
Keyword(s):  

1983 ◽  
Vol 133 (2) ◽  
pp. 327-333 ◽  
Author(s):  
Dominique LOMBARDO ◽  
Daniel CAMPESE ◽  
Luc MULTIGNER ◽  
Huguette LAFONT ◽  
Alain CARO

1986 ◽  
Vol 39 (2) ◽  
pp. 249 ◽  
Author(s):  
CJ Oconnor ◽  
ASH Mitha ◽  
P Walde

The pseudo-first-order rate constants of hydrolysis of a series of 4-nitrophenyl alkanoates and a series of n-alkyl esters of 4-nitrobenzoic acid and of 4-nitrophenyl hexahydrobenzoate and cyclohexyl 4-nitrobenzoate, catalysed by bile-salt-stimulated human milk lipase in the absence and presence (2 mmol dm-3) of sodium cholate/cholic acid and sodium taurocholate , have been measured at pH 7.3, 310.5 K. It has been shown that the enzyme possesses a specific esterase acyl binding site which almost completely excludes the binding therein of a cyclohexyl group. There is also present a specific alkyl binding site which can fully accommodate a cyclohexyl ring. Both binding sites are hydrophobic in nature, but although the hydrophobic nature of the alkyl binding site is affected by bile-salt stimulation, that of the acyl site is not. Hydrophobicity parameters have been calculated for hydrocarbon chains lying in the acyl and alkyl binding positions of bile-salt-stimulated human milk lipase.


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