Structure and Conformation of Human Pancreatic Carboxyl-Ester Hydrolase
1981; Wiley; Volume: 117; Issue: 3 Linguagem: Inglês
10.1111/j.1432-1033.1981.tb06360.x
ISSN1432-1033
AutoresOdette Guy, Dominique Lombardo, J. Brahms,
Tópico(s)Enzyme Catalysis and Immobilization
ResumoHuman pancreatic carboxyl‐ester hydrolase is a glycoprotein with a molecular weight of 100000 and a high content in carbohydrate, 20%. Sedimentation studies indicate that the molecule resembles an ellipsoid. The results of hydrodynamic and vacuum‐ultraviolet circular dichroism investigation allow one to propose a model of the carboxyl‐ester hydrolase three‐dimensional structure. The enzyme belongs to the ‘all β’ class of proteins; about 54–60% of its residues are in β‐sheets and in β‐turns, most probably forming the surface of an ellipsoid. A similarity with prealbumin structure is proposed and a comparison with structure of other pancreatic enzymes is presented.
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