Human liver GTP cyclohydrolase I: purification and some properties.
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Shen RS, Alam A, Zhang YX
Human liver GTP cyclohydrolase I: purification and some properties.
Biochimie. 1989 Mar;71(3):343-9.
- PubMed ID
- 2500984 [ View in PubMed]
- Abstract
Human liver guanosine triphosphate (GTP) cyclohydrolase I has been purified more than 1,700-fold to what appears to be homogeneity. The active enzyme complex has an estimated molecular weight of 453,000 +/- 11,500 by gel filtration chromatography. It consists of a polypeptide of 149,000 +/- 4,000 mol wt by SDS-polyacrylamide gel electrophoresis. The activity of the enzyme is heat stable and is inhibited by di- and trivalent cations. The enzyme has an optimum pH of 7.7 in sodium phosphate buffer. It uses GTP as a sole substrate, with a Km of 116 microM.