Abstract:
:The gene of an extreme thermophile, Thermus thermophilus HB8, which codes for a leucine biosynthetic enzyme, 3-isopropylmalate (3-IPM) dehydrogenase [EC 1.1.1.85], was cloned in Escherichia coli using pBR322 as a vector. E. coli cells carrying this recombinant plasmid, pHB2, produced the thermophilic enzyme 7-fold more than did T. thermophilus HB8 cells. When the crude extract of the pHB2-carrying cells was treated at 70 degrees C for 10 min, approximately 75% of the protein in the extract was precipitated with full activity of the thermophilic 3-IPM dehydrogenase being left in the supernatant, indicating that 4-fold purification was achieved during this process. This shows that the thermophilic 3-IPM dehydrogenase was purified 28-fold by these two procedures, cloning and heat treatment, and demonstrates that the extract from the plasmid-harboring cells is a good starting material for purification of the enzyme. Following the heat treatment, 3-IPM dehydrogenase was further purified by ammonium sulfate precipitation and DEAE-cellulose column chromatography. The enzyme preparation thus obtained contained 3-IPM dehydrogenase as a major component with a few minor impurities as shown by polyacrylamide gel electrophoresis, whereas the enzyme preparation from T. thermophilus HB8 cells obtained by the same procedures showed multiple bands on a polyacrylamide gel electrophoresis.
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Tanaka T,Kawano N,Oshima Tdoi
10.1093/oxfordjournals.jbchem.a133245subject
Has Abstractpub_date
1981-02-01 00:00:00pages
677-82issue
2eissn
0021-924Xissn
1756-2651journal_volume
89pub_type
杂志文章abstract::The activity of rat liver asparagine synthetase [EC 6.3.1.1]increased when animals maintained on 25% protein diet were placed on 15% or 6% protein diet. The enzyme activity level rose within one day, reached a maximum in 7 or 10 days after switching the diet and thereafter dropped gradually. During the purification of...
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pub_type: 杂志文章
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pub_type: 杂志文章
doi:10.1093/oxfordjournals.jbchem.a133088
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journal_title:Journal of biochemistry
pub_type: 杂志文章
doi:10.1093/oxfordjournals.jbchem.a132812
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更新日期:1989-10-01 00:00:00
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pub_type: 杂志文章
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更新日期:2009-04-01 00:00:00
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journal_title:Journal of biochemistry
pub_type: 杂志文章
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更新日期:1999-03-01 00:00:00
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journal_title:Journal of biochemistry
pub_type: 杂志文章
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更新日期:1995-06-01 00:00:00
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pub_type: 杂志文章
doi:10.1093/oxfordjournals.jbchem.a122380
更新日期:1988-06-01 00:00:00
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journal_title:Journal of biochemistry
pub_type: 杂志文章
doi:10.1093/jb/mvp107
更新日期:2009-10-01 00:00:00
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更新日期:2001-09-01 00:00:00
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journal_title:Journal of biochemistry
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更新日期:2000-10-01 00:00:00
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journal_title:Journal of biochemistry
pub_type: 杂志文章
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pub_type: 杂志文章,评审
doi:10.1093/oxfordjournals.jbchem.a124992
更新日期:1995-12-01 00:00:00
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更新日期:2010-10-01 00:00:00
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pub_type: 杂志文章
doi:10.1093/oxfordjournals.jbchem.a122212
更新日期:1988-01-01 00:00:00
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journal_title:Journal of biochemistry
pub_type: 杂志文章
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更新日期:2004-03-01 00:00:00
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journal_title:Journal of biochemistry
pub_type: 杂志文章
doi:10.1093/oxfordjournals.jbchem.a133877
更新日期:1982-05-01 00:00:00
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journal_title:Journal of biochemistry
pub_type: 杂志文章
doi:10.1093/oxfordjournals.jbchem.a122096
更新日期:1987-09-01 00:00:00