文献检索，用中文搜 PubMed

Suppr 超能文献

核心技术专利：CN118964589B侵权必究

核心技术专利：CN118964589B侵权必究

Biochem J. 1976 Mar 1;153(3):533-41. doi: 10.1042/bj1530533.

Nitrate reductase was purified 134-fold from Escherichia coli K12. The purification procedure involves the release by Triton X-100 of the enzyme from the cell envelope. i. The purified enzyme exists in aqueous solution either as a monomer (mol. wt. about 220 000) or as an associated form (probably a tetramer; mol.wt. about 880 000). 3. The purified enzyme has three subunits with apparent mol.wts. of 150 000, 67000 and 65000. An additional subunit of apparent mol.wt. 20000 is present in a haem-containing fraction that is also produced by the preparative procedure described. 4. None of the enzyme subunits is present in the cell envelope of cells grown in the absence of nitrate. 5. Reversible changes in the activity of nitrate reductase in vitro with FMNH2 as reductant can be induced under circumstances which are without effect on the reduced Benzyl Viologen-NO3-activity.

硝酸还原酶从大肠杆菌K12中纯化出来，纯化了134倍。纯化过程包括用Triton X-100将酶从细胞膜中释放出来。i. 纯化后的酶在水溶液中以单体形式（分子量约220000）或缔合形式（可能是四聚体；分子量约880000）存在。3. 纯化后的酶有三个亚基，表观分子量分别为150000、67000和65000。在通过所述制备过程产生的含血红素组分中还存在一个表观分子量为20000的额外亚基。4. 在无硝酸盐条件下生长的细胞的细胞膜中不存在任何酶亚基。5. 在对还原型苄基紫精 - NO3 - 活性无影响的情况下，体外以FMNH2作为还原剂可诱导硝酸还原酶活性发生可逆变化。

Biochem J. 1976 Mar 1;153(3):533-41. doi: 10.1042/bj1530533.

Nitrate reductase was purified 134-fold from Escherichia coli K12. The purification procedure involves the release by Triton X-100 of the enzyme from the cell envelope. i. The purified enzyme exists in aqueous solution either as a monomer (mol. wt. about 220 000) or as an associated form (probably a tetramer; mol.wt. about 880 000). 3. The purified enzyme has three subunits with apparent mol.wts. of 150 000, 67000 and 65000. An additional subunit of apparent mol.wt. 20000 is present in a haem-containing fraction that is also produced by the preparative procedure described. 4. None of the enzyme subunits is present in the cell envelope of cells grown in the absence of nitrate. 5. Reversible changes in the activity of nitrate reductase in vitro with FMNH2 as reductant can be induced under circumstances which are without effect on the reduced Benzyl Viologen-NO3-activity.

硝酸还原酶从大肠杆菌K12中纯化出来，纯化了134倍。纯化过程包括用Triton X-100将酶从细胞膜中释放出来。i. 纯化后的酶在水溶液中以单体形式（分子量约220000）或缔合形式（可能是四聚体；分子量约880000）存在。3. 纯化后的酶有三个亚基，表观分子量分别为150000、67000和65000。在通过所述制备过程产生的含血红素组分中还存在一个表观分子量为20000的额外亚基。4. 在无硝酸盐条件下生长的细胞的细胞膜中不存在任何酶亚基。5. 在对还原型苄基紫精 - NO3 - 活性无影响的情况下，体外以FMNH2作为还原剂可诱导硝酸还原酶活性发生可逆变化。