ATP-citrate lyase as a substrate of protein histidine phosphatase in vertebrates
ATP-citrate lyase as a substrate of protein histidine phosphatase in vertebrates
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DOI：
10.1016/s0006-291x(03)00920-3
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发表时间：
2003-06-20
影响因子：
3.1
通讯作者：
Krieglstein, J
中科院分区：
文献类型：
--
作者：
Klumpp, S;Bechmann, G;Krieglstein, J
最近发现的第一个来自脊椎动物的蛋白质组胺酸磷酸酶在多种组织中被发现，但缺少一种生理底物蛋白。磷酸化的肝提取物在EDTA的存在下，随后通过SDS-PAGE和放射自显影显示标记的三种蛋白质。酸和碱处理揭示了N-磷酸盐的存在。组氨酸磷酸酶的添加仅导致110 kDa蛋白质的去磷酸化（变性条件）。凝胶过滤显示其天然分子量约为450 kDa。该蛋白经纯化和鉴定为ATP-柠檬酸裂解酶。这些结果支持组氨酸磷酸酶在代谢过程中发挥重要但尚未确定的作用。(C)2003 Elsevier Science（美国）。All rights reserved.
The first protein histidine phosphatase from vertebrates discovered recently was found in a variety of tissues, however, a physiological substrate protein was missing. Phosphorylation of liver extracts in the presence of EDTA, followed by SDS-PAGE and autoradiography showed labeling of three proteins. Acid- and alkaline-treatment revealed the existence of N-phosphates. Addition of histidine phosphatase exclusively resulted in dephosphorylation of a 110 kDa protein (denaturing conditions). Gelfiltration revealed its native molecular mass of similar to450 kDa. That protein was purified and identified as ATP-citrate lyase. The results are in favor of histidine phosphatase playing an important yet unidentified role in metabolic processes. (C) 2003 Elsevier Science (USA). All rights reserved.