TY - JOUR
T1 - Purification and characterization of fructose-1,6-bisphosphatase from bovine brain
AU - Liu, Feng
AU - Fromm, Herbert J.
N1 - Funding Information:
1 This research was supported in part by Research Grant NS-10546 from the National Institutes of Health, United States Public Health Service, and Grant DMB-8502211 from the National Science Foundation. This is Journal Paper J-12656 of the Iowa Agriculture and Home Economics Experiment Station, Ames, IA, Project 2575. *A preliminary report of this study has been presented elsewhere (1).
PY - 1988/2/1
Y1 - 1988/2/1
N2 - 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.
AB - 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.
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U2 - 10.1016/0003-9861(88)90488-2
DO - 10.1016/0003-9861(88)90488-2
M3 - Article
C2 - 2829736
AN - SCOPUS:0023860806
VL - 260
SP - 609
EP - 615
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
SN - 0003-9861
IS - 2
ER -