DOPA decarboxylase inhibition through the interaction of coenzyme and substrate.
DOPA decarboxylase inhibition through the interaction of coenzyme and substrate.
复制标题
通过辅酶和底物的相互作用抑制多巴脱羧酶。
DOI：
10.1016/s0021-9258(18)55750-1
复制
发表时间：
1952
期刊：
影响因子：
--
通讯作者：
W. Clark
中科院分区：
文献类型：
--
作者：
H. F. Schott;W. Clark
方法采用Schales和Schales（1）的方法从新鲜豚鼠肾中制备酶。脱羧酶的活性进行了研究，在锥形瓦尔堡容器与两个侧臂。将酶粉末溶解在0.1M的pH6.8的磷酸盐缓冲液中，并将所需量的酶粉末与足够的缓冲液一起移液到容器的主室中，使最终体积为4.5ml。将底物L-多巴溶于水中，用移液管吸取到一侧臂中，0.3* 这项研究得到了美国公共卫生署国立卫生研究院研究赠款和奖学金处的H-658（C）资助。经退伍军人管理局审查，并经首席医疗主任批准后出版。作者的陈述和结论是他们自己研究的结果，不一定反映退伍军人管理局的意见或政策。
MethodsThe enzyme was prepared by the method of Schales and Schales (1): as a dry powder from fresh guinea pig kidneys. The decarboxylase activity was studied in conical Warburg vessels with two side arms. The enzyme powder was dissolved in 0.1 M phosphate buffer at pH 6.8 and the desired quantity pipetted into the main chamber of the vessel together with sufficient buffer to make the final volume 4.5 ml. The substrate, L-dopa, was dissolved in water and pipetted into one side arm, and 0.3* This investigation was supported by Grant H-658 (C) from the Division of Research Grants and Fellowships of the National Institutes of Health, United States Public Health Service. Reviewed by the Veterans Administration and published with the approval of the Chief Medical Director. The statements and conclusions of the authors are the result of their own study and do not necessarily reflect the opinion or policy of the Veterans Administration.