Abstract
The interaction of alpha 2 macroglobulin (alpha 2M) with exogenous proteases has been reported by others to be abnormal in cystic fibrosis (CF). We have re-examined these claims. Four parameters were considered:(1) the molar protease binding of alpha 2M; (2) the interaction of bovine cationic trypsin (BCT), complexed to alpha 2M, with low molecular mass substrate, benzoyl arginine ethyl ester (BAEE); (3) the stability of formed alpha 2 M-BCT complexes; and (4) the subunit structure of alpha 2M. We have found CF alpha 2M to be similar to control alpha 2M in every respect studied.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adolescent
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Anthraquinones
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Arginine / analogs & derivatives
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Arginine / metabolism
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Child
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Coloring Agents
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Cystic Fibrosis / metabolism*
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Female
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Humans
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Kinetics
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Macromolecular Substances
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Male
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Peptide Hydrolases / metabolism*
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Trypsin / metabolism
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Trypsin Inhibitor, Kunitz Soybean / metabolism
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alpha-Macroglobulins / metabolism*
Substances
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Anthraquinones
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Coloring Agents
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Macromolecular Substances
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alpha-Macroglobulins
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Trypsin Inhibitor, Kunitz Soybean
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Arginine
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benzoylarginine ethyl ester
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Peptide Hydrolases
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Trypsin
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Remazol Brilliant Blue R