ALG-2 divalent-ion affinity: Calorimetric analysis of the des23 versions reveals high-affinity site for Mg2 +
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- 作者：Michael T. Henzl ; henzlm@missouri.edu" class="auth_mail" title="E-mail the corresponding author ; Benjamin B. Frey ; Andrew J. Wolf
- 关键词：ABM ; ALG-2 binding motif ; EDTA ; ethylenediaminetetraacetic acid ; EGTA ; ethylene glycol-bis(β-aminoethyl ether)-N ; N ; N&rsquo ; N&rsquo ; -tetraacetic acid ; HBS ; Hepes ; 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid ; IPTG ; isopropyl-β-D-thiogalactopyranoside ; ITC ; isothermal titration calorimetry ; LB ; Luria-Bertani ; NTA ; nitrilotriacetic acid ; PAGE ; polyacrylamide gel electrophoresis ; PRR ; proline-rich region
- 刊名：Biophysical Chemistry
- 出版年：2016
- 出版时间：February 2016
- 年：2016
- 卷：209
- 期：Complete
- 页码：28-40
- 全文大小：2384 K
文摘
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ALG-2des23wt binds Ca2 + ions sequentially, with no apparent cooperativity.
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ALG-2des23ΔGF122 binds Ca2 + with evidence of inter-subunit cooperativity.
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Both isoforms possess a high-affinity (K > 5 × 104 M− 1) binding-site for Mg2 +.
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The high-affinity Mg2 + site exhibits atypically low affinity for Ca2 +.
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The Mg2 +-binding site is believed to reside in the EF5 binding loop.