The uncoupling protein from brown adipose tissue mitochondria is a dimer. A hydrodynamic study
The uncoupling protein from brown adipose tissue mitochondria is a dimer. A hydrodynamic study
复制标题
棕色脂肪组织线粒体的解偶联蛋白是二聚体。
DOI:
10.1016/0014-5793(80)80614-4
复制
发表时间:
1980
期刊:
影响因子:
3.5
通讯作者:
E.M. Klingenberg
中科院分区:
文献类型:
--
作者:
C.S. Lin;H. Hackenberg;E.M. Klingenberg
In the preceding paper we described the purification of a purine nucleotide binding protein from brown adipose tissue mitochondria which appears to be the uncoupling factor, peculiar to these mitochondria [11. The protein was obtained with more than 90% purity in relatively high yield associated with Triton X-100. The MW of its subunit was estimated by SDS gel electrophoresis to be 32 000. The solubilized protein has the same binding capacity for GDP as in mitochondria which indicates that the isolated protein has largely retained the native conformation. The number of binding sites for GDP was found to be 16 pmol/g protein, corresponding to a MW of 62 000. It was therefore suggested that the protein consists of a dimer of two subunits of 32 000 with one binding site of GDP. This case would be analogous to the ADP, ATP carrier of mitochondria which has a MW of 60 000 with two subunits of 30 000 and one binding site for carboxyatractylate [2-41.In the present paper we will present some data on the hydrodynamic properties of the isolated uncoupling protein with the aim of establishing its MW. In view of the analogy to the ADP, ATP carrier, the solubilized uncoupling protein can be expected to exist as a mixed protein Triton micelle with a high Triton content. Hydrodynamic measurements have to take into account the high content of Triton. Interference by Triton has been overcome according to the techniques described previously for the ADP, AT’P carrier [5, 6].