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<span style = 'font-size: large'> '''Bennett, CD, Rodkey, JA, Sondey, JM and Hirschmann, R''' (1978) Dihydrofolate reductase: the amino acid sequence of the enzyme from a methotrexate-resistant mutant of Escherichia coli.''Biochemistry'' '''17''':1328-37</span> | |||
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|{{TableHeadingColor}} |'''Abstract''' || <protect>The determination of the amino acid sequence of the enzyme dihydrofolate reductase (5,6,7,8-tetrahydrofolate:NADP+ oxidoreductase, EC 1.5.1.3) from a mutant of Escherichia coli B is described. The 159 residues were positioned by automatic Edman degradation of the whole protein, of the reduced and alkylated cyanogen bromide fragments, and of selected tryptic, chymotryptic, and thermolytic digestion products. An N-bromosuccinimide produced fragment of the largest cyanogen bromide peptide was also used in the sequence determination.</protect> | |||
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* [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=350268 PubMed] | |||
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==Significance {{HelpIcon|Help:Literature}} == | |||
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== Useful Materials and Methods {{HelpIcon|Help:Literature}}== | |||
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Revision as of 23:16, 25 June 2010
Bennett, CD, Rodkey, JA, Sondey, JM and Hirschmann, R (1978) Dihydrofolate reductase: the amino acid sequence of the enzyme from a methotrexate-resistant mutant of Escherichia coli.Biochemistry 17:1328-37
| Abstract | <protect>The determination of the amino acid sequence of the enzyme dihydrofolate reductase (5,6,7,8-tetrahydrofolate:NADP+ oxidoreductase, EC 1.5.1.3) from a mutant of Escherichia coli B is described. The 159 residues were positioned by automatic Edman degradation of the whole protein, of the reduced and alkylated cyanogen bromide fragments, and of selected tryptic, chymotryptic, and thermolytic digestion products. An N-bromosuccinimide produced fragment of the largest cyanogen bromide peptide was also used in the sequence determination. |
|- |bgcolor='#CCCCFF' nowrap |Links ||
|} </protect>
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