作者: N Ohno , D C Morrison
DOI: 10.1016/S0021-9258(18)83761-9
关键词: Affinity label 、 Polyacrylamide gel electrophoresis 、 Binding site 、 Non-competitive inhibition 、 Enzyme 、 Limulus 、 Lipopolysaccharide 、 Biochemistry 、 Lysozyme 、 Chemistry
摘要: Experiments have been carried out to characterize the binding of lysozyme (LZM) bacteriol lipopolysaccharide (LPS). The formation LPS·LZM complexes can be readily demonstrated using either physical-chemical separation techniques or a radiolabeled photoaffinity LPS probe. affinity LZM for has estimated ∼ 108 liters/mol. Binding results in loss enzymatic activity by noncompetitive inhibition, as assessed particulate soluble substrates. This interaction with is dictated primarily hydrophobic interactions and appears general property both constituents. human avian sources, well isolated from variety Gram-negative organisms. addition biologically relevant fluids containing dose-dependent inhibition suggesting that such may relevance infections. Finally shown reduce endotoxic gelation Limulus amoebocyte lysates.