Interactions of bivalent metal ions and bovine serum albumins

GAO Xingjun; GUO Ming; LI Bing; GUO Jianzhong; LI Minghui

doi:10.11833/j.issn.2095-0756.2013.05.022

Volume 30 Issue 5

Sep. 2013

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GAO Xingjun, GUO Ming, LI Bing, GUO Jianzhong, LI Minghui. Interactions of bivalent metal ions and bovine serum albumins[J]. Journal of Zhejiang A&F University, 2013, 30(5): 777-783. doi: 10.11833/j.issn.2095-0756.2013.05.022

Citation:

GAO Xingjun, GUO Ming, LI Bing, GUO Jianzhong, LI Minghui. Interactions of bivalent metal ions and bovine serum albumins[J]. Journal of Zhejiang A&F University, 2013, 30(5): 777-783. doi: 10.11833/j.issn.2095-0756.2013.05.022

Interactions of bivalent metal ions and bovine serum albumins

doi: 10.11833/j.issn.2095-0756.2013.05.022

1.
Faculty of Science，Zhejiang A & F University，Lin’an 311300，Zhejiang，China

More Information

Corresponding author: GAO Xingjun
Received Date: 2012-10-31
Rev Recd Date: 2013-01-09
Publish Date: 2013-10-20

Abstract

To obtain the principal of the interactions among bovine serum albumins（BSA）and the bivalent metal ions，the interactions of five bivalent metal ions（Zn2+，Ni2+，Co2+，Ca2+，and Mg2+），and BSA were studied using fluorescence spectroscopy and ultraviolet spectroscopy. Also, a quenching reaction mechanism of biomacromolecules was used with the site binding model, and quenching of the intrinsic fluorescence of BSA was found by adding Zn2+，Ni2+，Co2+，and Ca2+. For the appropriate ionic radius of Zn2+，Ni2+，and Co2+，a supramolecular complex was formed among the metal ions and BSA by effectively entering the binding site of the BSA. At the same time，the secondary structure of BSA was changed and manifested as static quenching. But the supramolecular complex could not be formed between BSA and Ca2+ for the influence of the steric hindrance due to a greater ionic radius of Ca2+. Additionally，since the metal ion Mg2+ had a much greater hydrated radius than the other divalent ions, an effective collision between Mg2+ and BSA was prevented. Therefore, the metal ion Ca2+ was only manifested as dynamic quenching, and metal ion Mg2+ had no quenching effect on the intrinsic fluorescence of BSA. Ca2+，Mg2+ other than the ions Zn2+, Ni2+，and Co2+，had no interactions with BSA.［Ch，3 fig. 2 tab. 16 ref.］
- zoology,
- metal ion（Ⅱ）,
- bovine serum albumin,
- fluorescence spectroscopy,
- ultraviolet spectrum

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通讯作者: 陈斌, bchen63@163.com

1.
沈阳化工大学材料科学与工程学院沈阳 110142

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Interactions of bivalent metal ions and bovine serum albumins

1. Faculty of Science，Zhejiang A & F University，Lin’an 311300，Zhejiang，China

Corresponding author: GAO Xingjun

Received Date: 2012-10-31

Rev Recd Date: 2013-01-09

Publish Date: 2013-10-20

Key words:

Abstract: To obtain the principal of the interactions among bovine serum albumins（BSA）and the bivalent metal ions，the interactions of five bivalent metal ions（Zn2+，Ni2+，Co2+，Ca2+，and Mg2+），and BSA were studied using fluorescence spectroscopy and ultraviolet spectroscopy. Also, a quenching reaction mechanism of biomacromolecules was used with the site binding model, and quenching of the intrinsic fluorescence of BSA was found by adding Zn2+，Ni2+，Co2+，and Ca2+. For the appropriate ionic radius of Zn2+，Ni2+，and Co2+，a supramolecular complex was formed among the metal ions and BSA by effectively entering the binding site of the BSA. At the same time，the secondary structure of BSA was changed and manifested as static quenching. But the supramolecular complex could not be formed between BSA and Ca2+ for the influence of the steric hindrance due to a greater ionic radius of Ca2+. Additionally，since the metal ion Mg2+ had a much greater hydrated radius than the other divalent ions, an effective collision between Mg2+ and BSA was prevented. Therefore, the metal ion Ca2+ was only manifested as dynamic quenching, and metal ion Mg2+ had no quenching effect on the intrinsic fluorescence of BSA. Ca2+，Mg2+ other than the ions Zn2+, Ni2+，and Co2+，had no interactions with BSA.［Ch，3 fig. 2 tab. 16 ref.］

Interactions of bivalent metal ions and bovine serum albumins

doi: 10.11833/j.issn.2095-0756.2013.05.022

Abstract

References

Proportional views

通讯作者: 陈斌, bchen63@163.com

Related

Proportional views