Takayama K, Kudo I, Hara S, Murakami M, Matsuta K, Miyamoto T, Inoue K
Department of Health Chemistry, Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
Biochem Biophys Res Commun. 1990 Mar 30;167(3):1309-15. doi: 10.1016/0006-291x(90)90666-b.
Four monoclonal antibodies (HP-1, HP-2, HP-3 and HP-4) with differing reactivities were raised against human synovial fluid phospholipase A2. None of them bound to exocrine phospholipases A2, such as those from pancreas or snake venom. However, antibodies HP-1 and HP-3 showed cross-reactivity with rabbit and rat platelet secretory phospholipases A2, which share common enzymatic and structural features with the human synovial enzyme. Antibodies HP-1, HP-2 and HP-3 inhibited the activity of human synovial phospholipase A2. The antibodies were used to develop a rapid immunoaffinity column chromatographic procedure for enzyme purification. In some preparations, the recovery of total activity after immunoaffinity column chromatography was more than 100% suggesting the existence of endogenous inhibitory factors of phospholipase A2 in human synovial fluid.
针对人滑液磷脂酶A2制备了四种反应性不同的单克隆抗体（HP-1、HP-2、HP-3和HP-4）。它们均不与外分泌性磷脂酶A2结合，如来自胰腺或蛇毒的磷脂酶A2。然而，抗体HP-1和HP-3与兔和大鼠血小板分泌性磷脂酶A2呈现交叉反应，这些酶与人类滑膜酶具有共同的酶学和结构特征。抗体HP-1、HP-2和HP-3可抑制人滑液磷脂酶A2的活性。这些抗体被用于开发一种用于酶纯化的快速免疫亲和柱色谱方法。在某些制剂中，免疫亲和柱色谱后总活性的回收率超过100%，这表明人滑液中存在磷脂酶A2的内源性抑制因子。
