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Conformational changes of the α 1 ‐proteinase inhibitor affecting its cholesterol binding ability
Author(s) -
Janciauskiene Sabina,
Eriksson Sten
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81347-3
Subject(s) - chemistry , cysteine , pancreatic elastase , trypsin , in vitro , biochemistry , thiol , peptide , alpha (finance) , cholesterol , elastase , glutathione , conformational change , cleavage (geology) , cystine , stereochemistry , enzyme , biology , paleontology , fracture (geology) , medicine , construct validity , nursing , patient satisfaction
The effect of conformational changes of the α 1 ‐proteinase inhibitor (α 1 pI) on α 1 PI‐cholesterol complex (1:2 mol/mol) formation in vitro was studied with electrophoretic and gel Chromatographic methods. Native α 1 PI was modified by adding free thiol agents such as glutathione, cysteine HCl, or dl ‐homocysteine, by heating, or by cleavage with pancreatic elastase or trypsin. Conformational changes of the α 1 PI molecule induced by these procedures were all accompanied by a loss of its ability to bind cholesterol in vitro under standard experimental conditions. The data suggest α 1 PI‐cholesterol binding to be affected by both direct and indirect modifications of the α 1 PI‐reactive center, that is situated on a mobile peptide loop.