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Article

Immobilization of dihydrofolate reductase by engineered cysteine residue attached to its C-terminal end.

Journal of biochemistry - 1 Sept 1993

Iwakura M, Kokubu T

Abstract excerpt

A cysteine residue with a short amino acid chain spacer was attached to the C-terminal end of mutant dihydrofolate reductase [DHFR(C152E)] by a recombinant DNA technique. By using 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) as a SH reagent, it was determined that the reactivity of the SH group of the introduced C-terminal cysteine was much higher than that of cysteines with the wild-type DHFR (C85 and C152),...

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Source

Identifiers

PMID: 8282723
DOI: 10.1093/oxfordjournals.jbchem.a124178

Genes

DHFR
DTNB

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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