Structure and Conformation of Human Pancreatic Carboxyl‐Ester Hydrolase
Open Access
- 1 July 1981
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 117 (3) , 457-460
- https://doi.org/10.1111/j.1432-1033.1981.tb06360.x
Abstract
Human pancreatic carboxyl-ester hydrolase is a glycoprotein with a MW of 100,000 and a high content in carbohydrate, 20%. Sedimentation studies indicate that the molecule resembles an ellipsoid. The results of hydrodynamic and vacuum-UV circular dichroism investigation allows a model of the carboxyl-ester hydrolase 3-dimensional structure to be proposed. The enzyme belongs to the all .beta. class of proteins; 54-60% of its residues are in .beta.-sheets and in .beta.-turns, 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.This publication has 26 references indexed in Scilit:
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