Purification and characterization of fructose-1,6-bisphosphatase from bovine brain

Feng Liu, Herbert J. Fromm

Research output: Contribution to journalArticle

32 Citations (Scopus)

Abstract

Fructose-1,6-bisphosphatase from bovine brain tissue has been purified to near homogeneity. This enzyme is similar to other mammalian fructose-1,6-bisphosphatases in many respects, and its properties are distinctly different from those reported for the enzyme from rat brain [A. L. Majumder and F. Eisenberg (1977) Proc. Natl Acad. Sci. USA 74, 3222-3225;S. Chattoraj and A. L. Majumder (1986) Biochem. Biophys. Res. Commun.139, 571-580]. The bovine enzyme (sp act 4, pH ratio ( 7.5 9.6) = 3.6) has a pH optimum of 7.5. The Km is 2 μm. Divalent metal ion is required for activity, and Vmax is obtained at either 4 mm Mg2+ or 0.3 mm Mn2+. Fructose 2,6-bisphosphate is a competitive inhibitor (Ki = 0.07 μM), and AMP a noncompetitive inhibitor (kis = 24 μM, Kii = 10 μM) of bovine brain fructose-1,6-bisphosphatase. The enzyme activity is enhanced by small amounts of EDTA relative to metal, and AMP inhibits fructose-1,6-bisphosphatase in either the presence or absence of the metal chelator; however, AMP is more effective in the absence of EDTA.

Original languageEnglish (US)
Pages (from-to)609-615
Number of pages7
JournalArchives of Biochemistry and Biophysics
Volume260
Issue number2
DOIs
StatePublished - Feb 1 1988
Externally publishedYes

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Fructose-Bisphosphatase
Adenosine Monophosphate
Purification
Brain
Edetic Acid
Metals
Enzymes
Enzyme activity
Chelating Agents
Fructose
Metal ions
Rats
Tissue
Ions

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Purification and characterization of fructose-1,6-bisphosphatase from bovine brain. / Liu, Feng; Fromm, Herbert J.

In: Archives of Biochemistry and Biophysics, Vol. 260, No. 2, 01.02.1988, p. 609-615.

Research output: Contribution to journalArticle

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