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Development of a merP protein-based ...
~
Stapleton, James Mark.
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Development of a merP protein-based biotechnology for the selective removal of mercury from contaminated wastestreams.
紀錄類型:
書目-電子資源 : Monograph/item
正題名/作者:
Development of a merP protein-based biotechnology for the selective removal of mercury from contaminated wastestreams./
作者:
Stapleton, James Mark.
面頁冊數:
99 p.
附註:
Source: Dissertation Abstracts International, Volume: 57-10, Section: B, page: 6155.
Contained By:
Dissertation Abstracts International57-10B.
標題:
Environmental Sciences. -
電子資源:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9710097
ISBN:
0591175495
Development of a merP protein-based biotechnology for the selective removal of mercury from contaminated wastestreams.
Stapleton, James Mark.
Development of a merP protein-based biotechnology for the selective removal of mercury from contaminated wastestreams.
- 99 p.
Source: Dissertation Abstracts International, Volume: 57-10, Section: B, page: 6155.
Thesis (Ph.D.)--Michigan Technological University, 1996.
This study proposes to develop an innovative technique for the removal of mercury from Wastestreams which is based upon the isolation of the natural merP protein found in many bacterial systems. Additionally, to further our understanding of how the merP protein will behave in the variable wastestream environment, an analysis of the physical and chemical characterics of Hg+2 binding to the merP protein will also be preformed.
ISBN: 0591175495Subjects--Topical Terms:
676987
Environmental Sciences.
Development of a merP protein-based biotechnology for the selective removal of mercury from contaminated wastestreams.
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Development of a merP protein-based biotechnology for the selective removal of mercury from contaminated wastestreams.
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Source: Dissertation Abstracts International, Volume: 57-10, Section: B, page: 6155.
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Advisers: J. R. Mihelcic; D. R. Lueking.
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Thesis (Ph.D.)--Michigan Technological University, 1996.
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This study proposes to develop an innovative technique for the removal of mercury from Wastestreams which is based upon the isolation of the natural merP protein found in many bacterial systems. Additionally, to further our understanding of how the merP protein will behave in the variable wastestream environment, an analysis of the physical and chemical characterics of Hg+2 binding to the merP protein will also be preformed.
520
$a
A proprietary strain of Escherichia coli (strain LE392 possessing plasmid pKL156) which possesses a cloned merROPTP
$\
Delta
520
$a
The purity and identity of the protein were examined by native and denaturing polyacrylamide gel electrophoresis and N-terminal analysis and amino acid compositional analysis and agreed with the values reported in literature. Chemical reduction of the oxidized form of the merP protein was not possible and auto-oxidation of the purified protein was determined to be negligible which is in agreement with Sahlman and Jonsson (1992). The binding of mercury by the merP protein is relatively insensitive to pH variation between 6.5 and 8.5 and is thermally stable up to 40
$\
sp\circ
$\
rm\sb{d}
$
of 2. 1 uM and total binding capacity of 3.7 uM for a system containing 3.6 uM reduced protein. This finding is generally consistent with Sahlman and Jonsson's (1992) apparent K
$\
rm\sb{d}
$
of 3.7 uM and a total binding capacity of 8.8 uM for a system with 10 uM reduced protein. Future engineering significance for mercury removal are discussed.
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http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9710097
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