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Isolation, reconstitution, and molec...

Bu, Jia-Ying Juan.

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Isolation, reconstitution, and molecular cloning of the manganese-containing superoxide dismutase from Deinococcus radiodurans.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Isolation, reconstitution, and molecular cloning of the manganese-containing superoxide dismutase from Deinococcus radiodurans./
作者:	Bu, Jia-Ying Juan.
面頁冊數:	209 p.
附註:	Source: Dissertation Abstracts International, Volume: 53-02, Section: B, page: 0690.
Contained By:	Dissertation Abstracts International53-02B.
標題:	Biology, Molecular. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9220626

Isolation, reconstitution, and molecular cloning of the manganese-containing superoxide dismutase from Deinococcus radiodurans.
Bu, Jia-Ying Juan.

Isolation, reconstitution, and molecular cloning of the manganese-containing superoxide dismutase from Deinococcus radiodurans. - 209 p.

Source: Dissertation Abstracts International, Volume: 53-02, Section: B, page: 0690.

Thesis (Ph.D.)--Virginia Polytechnic Institute and State University, 1992.

The superoxide dismutase from a radiation-resistant bacterium Deinococcus radiodurans has been purified to electrophoretic homogeneity. The superoxide dismutase has a specific activity of 3300 units/mg and an apparent molecular mass of 43,000 daltons. The enzyme contains 1.5 gram-atom of manganese per mol dimer, and is composed of two identical subunits of 23,500 daltons. The enzyme rapidly loses its catalytic activity and metal content upon dialysis in denaturing reagent, guanidine hydrochloride, and the metal ion chelator 8-hydroxyquinoline. The denatured apoprotein was renatured upon removal of the denaturant by dialysis. The renatured apoprotein assumed a gross conformation similar to the native enzyme as indicated by fluorescence spectroscopy. The renatured apoprotein was reconstituted to the native specific activity upon addition of manganese in the absence of denaturant. The manganese reconstituted enzyme contained 1.7 gram-atom of manganese per mol dimer, and had a specific activity of 3650 units/mg. Kinetic studies revealed that the reconstitution with manganese was pH-dependent, and was inhibited by competing metal ions (iron and zinc).Subjects--Topical Terms:

1017719
Biology, Molecular.

Isolation, reconstitution, and molecular cloning of the manganese-containing superoxide dismutase from Deinococcus radiodurans.
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100 1 $a Bu, Jia-Ying Juan. $3 1949561
245 1 0 $a Isolation, reconstitution, and molecular cloning of the manganese-containing superoxide dismutase from Deinococcus radiodurans.
300 $a 209 p.
500 $a Source: Dissertation Abstracts International, Volume: 53-02, Section: B, page: 0690.
500 $a Chairman: Eugene M. Gregory.
502 $a Thesis (Ph.D.)--Virginia Polytechnic Institute and State University, 1992.
520 $a The superoxide dismutase from a radiation-resistant bacterium Deinococcus radiodurans has been purified to electrophoretic homogeneity. The superoxide dismutase has a specific activity of 3300 units/mg and an apparent molecular mass of 43,000 daltons. The enzyme contains 1.5 gram-atom of manganese per mol dimer, and is composed of two identical subunits of 23,500 daltons. The enzyme rapidly loses its catalytic activity and metal content upon dialysis in denaturing reagent, guanidine hydrochloride, and the metal ion chelator 8-hydroxyquinoline. The denatured apoprotein was renatured upon removal of the denaturant by dialysis. The renatured apoprotein assumed a gross conformation similar to the native enzyme as indicated by fluorescence spectroscopy. The renatured apoprotein was reconstituted to the native specific activity upon addition of manganese in the absence of denaturant. The manganese reconstituted enzyme contained 1.7 gram-atom of manganese per mol dimer, and had a specific activity of 3650 units/mg. Kinetic studies revealed that the reconstitution with manganese was pH-dependent, and was inhibited by competing metal ions (iron and zinc).
520 $a The nucleotide and peptide sequences of this manganese-containing superoxide dismutase were determined by molecular cloning of the structural gene. The polymerase chain reaction (PCR) was employed for the amplification of the target superoxide dismutase gene, and two degenerate oligonucleotide primers were used. Primer SOD1 was deduced from the N-terminal peptide sequence of the D. radiodurans SOD; and primer SOD2 was deduced from the peptide sequence homologous in all of the superoxide dismutases. The amplified PCR fragment, 500 bases in length, was subcloned and sequenced, and the deduced peptide sequence confirmed the presence of the D. radiodurans superoxide dismutase coding sequence. The full length superoxide dismutase clone was obtained by probing the lambda EMBL3 genomic library with the radiolabeled PCR fragment. The sequence determination of the full length D. radiodurans superoxide dismutase clone identified an open reading frame of 630 nucleotides which encoded a peptide having a molecular mass of 23,347. The deduced peptide sequence shared 70% identity with that of the E. coli MnSOD. The sequence that could potentially form a hair-pin structure was observed at the 3 $\ sp\prime $- untranslated region of the gene. This structure may be involved in the stabilization of the messenger RNA.
590 $a School code: 0247.
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Biology, Microbiology. $3 1017734
690 $a 0307
690 $a 0410
710 2 0 $a Virginia Polytechnic Institute and State University. $3 1017496
773 0 $t Dissertation Abstracts International $g 53-02B.
790 1 0 $a Gregory, Eugene M., $e advisor
790 $a 0247
791 $a Ph.D.
792 $a 1992
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9220626