...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Clinical Chemistry: Journal of the American Association for Clinical Chemists >Rapid loss of lactate dehydrogenase isoenzyme activity in serum by cold-induced formation of immunoglobulin G-lactate dehydrogenase complex.
【24h】

Rapid loss of lactate dehydrogenase isoenzyme activity in serum by cold-induced formation of immunoglobulin G-lactate dehydrogenase complex.

机译：通过冷诱导形成免疫球蛋白G-乳酸脱氢酶复合物，血清中的乳酸脱氢酶同工酶活性迅速丧失。

获取原文
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Lactate dehydrogenase (LD; EC 1.1.1.27) activity in serum from a patient recovering from a myocardial infarction was extremely unstable when stored at 0 degree C. The activity of each LD isoenzyme except LD-1 decreased by at least 40% when serum was stored at 0 degree C for 4 h. The patient's erythrocyte LD activity had normal stability at lower temperatures, but LD from other sources, when added to the patient's serum, rapidly lost activity at 0 degree C. The patient's serum contained an immunoglobulin G that combined--at 0 degree C but not at 21 degrees C--primarily with LD isoenzymes containing one or more M subunits. Because this immunoglobulin-LD complex has no enzyme activity, we used 125I-labeled purified LD to study formation of the complex. NAD+ blocked the formation of immunoglobulin-LD complex but could not dissociate the complex and restore the LD activity.
机译：于0摄氏度保存时，从心肌梗塞恢复的患者血清中的乳酸脱氢酶（LD; EC 1.1.1.27）活性极为不稳定。在0摄氏度下保存4小时。患者的红细胞LD活性在较低的温度下具有正常的稳定性，但其他来源的LD添加到患者的血清中后，在0摄氏度时会迅速丧失活性。患者的血清中所含的免疫球蛋白G在0摄氏度时结合在一起，但没有在21摄氏度时-主要是含有一个或多个M亚基的LD同工酶。由于该免疫球蛋白-LD复合物没有酶活性，因此我们使用125 I标记的纯化的LD来研究复合物的形成。 NAD +阻止了免疫球蛋白-LD复合物的形成，但无法解离复合物并恢复LD活性。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号