Human liver GTP cyclohydrolase I: purification and some properties

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...

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Veröffentlicht in:	Biochimie 1989-03, Vol.71 (3), p.343-349
Hauptverfasser:	Shen, Rong-Sen, Alam, Aftab, Zhang, Yixian
Format:	Artikel
Sprache:	eng
Schlagworte:	Aminohydrolases - isolation & purification Analytical, structural and metabolic biochemistry Biological and medical sciences Centrifugation, Density Gradient Chromatography, Liquid Electrophoresis, Polyacrylamide Gel Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology GTP Cyclohydrolase - isolation & purification GTP cyclohydrolase I/ molecular weight/ subunit structure Hot Temperature Humans Hydrolases liver Liver - enzymology man Molecular Weight
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Zusammenfassung:	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-polycrylamide gel electrophoresis. The activity of the enyzme 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 K m of 116 μM.
ISSN:	0300-9084 1638-6183
DOI:	10.1016/0300-9084(89)90006-0