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Article

Isolation and characterization of GTP cyclohydrolase I from mouse liver. Comparison of normal and the hph-1 mutant.

The Journal of biological chemistry - 5 Jul 1991

Cha K W, Jacobson K B, Yim J J

Abstract excerpt

GTP cyclohydrolase I, an enzyme that catalyzes the first reaction in the pathway for the biosynthesis of pterin compounds, was purified from of C3H mouse liver by 192-fold to apparent homogeneity, using Ultrogel AcA34, DEAE-Trisacryl, and GTP-agarose gels. Its native molecular weight was estimated at 362,000. When the enzyme was subjected to electrophoresis on a denaturing polyacrylamide gel, only one protein...

Topics

Animals
Blotting, Western
Chromatography, Liquid
Electrophoresis, Polyacrylamide Gel
GTP Cyclohydrolase
Hydrogen-Ion Concentration
Immunodiffusion
Liver
Mice
Mutation
Spectrometry, Fluorescence

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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PMID: 1905717

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1905717-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Isolation and characterization of GTP cyclohydrolase I from mouse liver. Comparison of normal and the hph-1 mutant.PMID 1905717Read ↗

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