Literature DB >> 7285899

Structure and conformation of human pancreatic carboxyl-ester hydrolase.

O Guy, D Lombardo, J G Brahms.   

Abstract

Human pancreatic carboxyl-ester hydrolase is a glycoprotein with a molecular weight 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-ultraviolet circular dichroism investigation allow one to propose a model of the carboxyl-ester hydrolase three-dimensional structure. The enzyme belongs to the "all beta" class of proteins; about 54-60% of its residues are in beta-sheets and in beta-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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Year:  1981        PMID: 7285899     DOI: 10.1111/j.1432-1033.1981.tb06360.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  4 in total

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

Authors:  A Negre-Salvayre; N Abouakil; D Lombardo; R Salvayre
Journal:  Lipids       Date:  1990-08       Impact factor: 1.880

2.  Association of bile-salt-dependent lipase with membranes of human pancreatic microsomes is under the control of ATP and phosphorylation.

Authors:  E Pasqualini; N Caillol; E Mas; N Bruneau; D Lexa; D Lombardo
Journal:  Biochem J       Date:  1997-10-15       Impact factor: 3.857

3.  Carbohydrate structure of human pancreatic elastase 1.

Authors:  P Wendorf; D Linder; A Sziegoleit; R Geyer
Journal:  Biochem J       Date:  1991-09-01       Impact factor: 3.857

4.  Human fetoacinar pancreatic protein: an oncofetal glycoform of the normally secreted pancreatic bile-salt-dependent lipase.

Authors:  E Mas; N Abouakil; S Roudani; F Miralles; O Guy-Crotte; C Figarella; M J Escribano; D Lombardo
Journal:  Biochem J       Date:  1993-01-15       Impact factor: 3.857

  4 in total

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