Retention mechanism of lactate dehydrogenase in anion-exchange chromatography.
Retention mechanism of lactate dehydrogenase in anion-exchange chromatography.
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阴离子交换色谱中乳酸脱氢酶的保留机制。
DOI：
10.1016/s0021-9673(00)94032-9
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发表时间：
1987
期刊：
影响因子：
--
通讯作者：
Regnier,FE
中科院分区：
文献类型：
--
作者：
Drager,RR;Regnier,FE
研究了乳酸脱氢酶（LDH）同工酶在肌(M)亚基不被吸附基质保留的条件下阴离子交换保留机制。使用保留的化学计量位移模型来定量蛋白质上与吸附基质相互作用的离子基团的数量（Zn），确定LDH同工酶的Zn随着心脏(H)亚基的数量增加而增加，总共增加到三个H亚基。mh3和h4同工酶具有相同的zn。由于这种四聚体酶的亚基排列成四面体结构，这些数据表明，空间限制阻止任何超过三个亚基同时与吸附剂表面相互作用。mh3和h4同工酶之所以能够分离，显然是因为h4同工酶中存在多个等效面，相对于mh3同工酶，这既增加了h4的吸附概率和吸附速率，又降低了h4的解吸概率和解吸速率。从这些研究中得出结论，生物聚合物的三维结构将决定那些能够与吸附表面相互作用的表面残基，并且蛋白质的多个亚基或结构域可能在生物聚合物-表面相互作用中协同作用相当远。
The anion-exchange retention mechanism of lactate dehydrogenase (LDH) isoenzymes was examined under conditions where the muscle (M) subunit was not retained by the sorbent matrix. Using the stoichiometric displacement model of retention to quantitate the number (Zn) of ionic groups on the protein that interact with the sorbent matrix, it was determined thatZnfor the LDH isoenzymes increases incrementally as the number of heart (H) subunits is increased up to a total of three H subunits. Both the MH3and H4isoenzymes have the sameZn. As the subunits in this tetrameric enzyme are arranged in a tetrahedral structure, these data indicate that steric limitations prevent any more than three subunits from interacting simultaneously with the sorbent surface. The reason why the MH3and H4isoenzymes could be separated is apparently that there are multiple equivalent faces in the H4isoenzyme, and this both increases the probability and rate of adsorption and decreases the probability and rate of desorption for the H4relative to the MH3isoenzyme.It was concluded from these studies that the three-dimensional structure of a biopolymer will determine those surface residues which are in a position to interact with a sorbent surface and that multiple subunits or domains of a protein may act cooperatively over considerable distances in biopolymer—surface interactions.
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字母：某些脱氢酶中的分子对称轴和亚基界面。
影响因子：
5.6
作者：
Michael G. Rossmann;Margaret J. Adams;Manfred Buehner;Geoffrey C. Ford;Marvin L. Hackert;Anders Liljas;S. Rao;Leonabd J. Banaszak;Edward J. Hill;Demetrius Tsernoglou;Laurence Webb
通讯作者：
Laurence Webb
DOI：
10.1016/0021-9673(86)80059-0
发表时间：
1986
期刊：
Journal of chromatography
影响因子：
--
作者：
Lu,XM;Benedek,K;Karger,BL
通讯作者：
Karger,BL
影响因子：
5.6
作者：
GRAU, UM;TROMMER, WE;ROSSMANN, MG
通讯作者：
ROSSMANN, MG
DOI：
10.1016/0021-9673(86)80068-1
发表时间：
1986-05-30
期刊：
JOURNAL OF CHROMATOGRAPHY
影响因子：
--
作者：
FAUSNAUGH, JL;REGNIER, FE
通讯作者：
REGNIER, FE
小鼠睾丸乳酸脱氢酶同工酶 C4 的结构，分辨率为 2.9 A。
DOI：
10.2210/pdb1ldx/pdb
发表时间：
1978
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
W. D. Musick;M. Rossmann
通讯作者：
M. Rossmann