Lipopolysaccharide interaction with lysozyme. Binding of lipopolysaccharide to lysozyme and inhibition of lysozyme enzymatic activity.
Lipopolysaccharide interaction with lysozyme. Binding of lipopolysaccharide to lysozyme and inhibition of lysozyme enzymatic activity.
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发表时间：
1989-03
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通讯作者：
Naohito Ohno;David;-C.;Morrison
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作者：
Naohito Ohno;David;-C.;Morrison
实验研究了溶菌酶（LZM）与细菌脂多糖（LPS）的结合特性。LPS.LZM复合物的形成可以使用物理化学分离技术或放射性标记的光亲和LPS探针容易地证明。LZM对LPS的结合亲和力估计约为10（8）升/摩尔。通过颗粒或可溶性底物评估，LPS的结合导致LZM酶活性通过非竞争性抑制而丧失。LPS与LZM的这种相互作用主要由疏水相互作用决定，并且似乎是两种成分的一般性质。可以用人和禽类来源的LZM以及用从多种革兰氏阴性生物体分离的LPS证明结合。向含有LZM的生物学相关液体中添加LPS导致LZM酶活性的剂量依赖性抑制，表明这种相互作用可能与革兰氏阴性菌感染相关。最后，通过鲎变形细胞裂解物的凝胶化评估，已显示LZM降低LPS的内毒素活性。
Experiments have been carried out to characterize the binding of lysozyme (LZM) to bacteriol lipopolysaccharide (LPS). The formation of LPS.LZM complexes can be readily demonstrated using either physical-chemical separation techniques or a radiolabeled photoaffinity LPS probe. The binding affinity of LZM for LPS has been estimated to be approximately 10(8) liters/mol. Binding of LPS results in loss of LZM enzymatic activity by a noncompetitive inhibition, as assessed by either particulate or soluble substrates. This interaction of LPS with LZM is dictated primarily by hydrophobic interactions and appears to be a general property of both constituents. Binding can be demonstrated with LZM of both human and avian sources, as well as with LPS isolated from a variety of Gram-negative organisms. The addition of LPS to biologically relevant fluids containing LZM results in dose-dependent inhibition of LZM enzymatic activity suggesting that such interactions may have relevance in Gram-negative infections. Finally LZM has been shown to reduce the endotoxic activity of LPS as assessed by gelation of Limulus amoebocyte lysates.