Home LiteratureArticle Details
PMID: 350268 Published · ppublish English Journal Article

Dihydrofolate reductase: the amino acid sequence of the enzyme from a methotrexate-resistant mutant of Escherichia coli.

Biochemistry ·Vol. 17 ·No. 7 ·1978-04-04 ·Pages 1328-37

Bennett CD, Rodkey JA, Sondey JM, Hirschmann R

Abstract

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.

MeSH Terms
Amino Acid Sequence Cyanogen Bromide Drug Resistance, Microbial Escherichia coli/enzymology Methotrexate/pharmacology Mutation Peptide Fragments Tetrahydrofolate Dehydrogenase
Chemicals
Peptide Fragments Tetrahydrofolate Dehydrogenase Cyanogen Bromide Methotrexate
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Bennett C D
Rodkey J A
Sondey J M
Hirschmann R
Article Info
Journal
Biochemistry
Abbr.
Biochemistry
ISSN
0006-2960
Published
1978-04-04
Pages
1328-37
Language
English
Region
United States
NLM ID
0370623
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]