Characterization of hexokinase from wheat roots and its inhibition by aluminum. [Tritium aestivum]

Journal Article · Tue Apr 01 04:00:00 EST 1986 · Plant Physiol., Suppl.; (United States)

OSTI ID:6937420

Whitman, C E; Caldwell, C R

Hexokinase (HK) performs an important phosphate transfer function in the cell and may be a principal site of aluminum toxicity in plants. Therefore HK was partially purified from the roots of Al-tolerant and Al-sensitive wheat (Triticum aestivum) and its activity characterized. Double reciprocal plots of glucose phosphorylating activity were nonlinear. Localization of glucokinase activity in non-denaturing polyacrylamide gel electrophoresis (PAGE) confirmed the presence of two isozymes. Fructose phosphorylating activity exhibited simple linear kinetics, but non-denaturing PAGE resolved two isozymes. Aluminum had no effect on glucokinase at pH 7.9 but inhibited activity at pH 6.7; fructokinase was not inhibited at either pH. A comparison of the kinetic characteristics of HK from Al-tolerant and Al-sensitive wheat will be presented.

• Research Organization: Beltsville, MD
• OSTI ID: 6937420
• Journal Information: Plant Physiol., Suppl.; (United States), Journal Name: Plant Physiol., Suppl.; (United States) Vol. 80:4; ISSN PPYSA
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
ALUMINIUM
CEREALS
CHEMICAL REACTIONS
ELECTROPHORESIS
ELEMENTS
ENZYME ACTIVITY
ENZYMES
GRASS
HEXOKINASE
INHIBITION
METALS
PH VALUE
PHOSPHORUS-GROUP TRANSFERASES
PHOSPHORYLATION
PHOSPHOTRANSFERASES
PLANT CELLS
PLANTS
ROOTS
TOXICITY
TRANSFERASES
WHEAT