Cytoflowmetric analysis of binding pattern and a new binding kinetic constant for an enterovirus and receptor.
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概要
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A bovine enterovirus (MZ-468) was adsorbed to Sarcoma-180 cells at 4°C. The cells were reacted with FITC-labeled IgG antibody for the virus and were studied with a laser fluorescence cytoflowmeter. From the histograms, binding-saturation of receptors was observed and the dissociation constant (Kd) was estimated. A new binding rate constant was deduced from the change of the ratio of virus-adsorbed cells against time and virus concentration. The constant has a dimensions of (cm<SUP>3</SUP>/min·receptor-site) and probably represents the receptor class on a cell with the highest rate constant.
- 久留米大学医学部 The Kurume Medical Journal 編集部の論文
著者
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CHINAMI MASANOBU
Department of Gynecology and Obstetrics, Kurume University, School of Nedicine
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SHINGU MASAHISA
Department o f Microbiology, Kurume University School of Medicine
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