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Immunoglobulins and α1‐acid glycoprotein do not contribute to the cholesterol crystallization—promoting effect of concanavalin a—binding biliary protein
Author(s) -
A. C. Marianne,
Mok Kam S.,
Out Tiny,
Tytgat Guido N. J.,
Groen Albert K.
Publication year - 1994
Publication title -
hepatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.488
H-Index - 361
eISSN - 1527-3350
pISSN - 0270-9139
DOI - 10.1002/hep.1840200312
Subject(s) - concanavalin a , glycoprotein , antibody , fibronectin , cholesterol , biochemistry , chemistry , affinity chromatography , biology , in vitro , immunology , enzyme , extracellular matrix
Human bile contains cholesterol crystallization—stimulating proteins that can be isolated by concanavalin A—Sepharose chromatography. In the past few years an increasing number of different pronucleating proteins have been identified in the concanavalin A—binding fraction. In this study we attempted to estimate the relative contribution of a number of these proteins to total concanavalin A—binding pronucleating activity. For this purpose, concanavalin A—binding glycoproteins were isolated from gallbladder bile samples from 12 patients with gallstones. The role of IgA, IgG and IgM and α 1 ‐acid glycoprotein was investigated by means of immunoextraction. No decrease in crystallization‐promoting activity was observed after precipitation of more than 98% of the different immunoglobulins. In addition, removal of more than 95% of α 1 ‐acid glycoprotein from different concanavalin A—binding fractions had no significant effect on cholesterol crystallization—promoting activity. The influence of fibronectin was estimated by addition of physiological concentrations to a model bile system. At these concentrations fibronectin did not promote crystallization. From these data we conclude that immunoglobulins, α 1 ‐acid glycoprotein and probably also fibronectin do not significantly contribute to total concanavalin A—binding activity. (H EPATOLOGY 1994;20:626–632).