Abstract
ADPGlucose pyrophosphorylase A was purified 126-fold to homogeneity from maize endosperm. The molecular weight estimated by gel filtration was 375,000 and 400,000 by disc acrylamide electrophoretic techniques. SDS disc gel electrophoresis showed a single protein band suggesting a monomeric molecular weight of 96,000. Thus, it was concluded that ADPGlucose pyrophosphorylase A in maize endosperm consists as a tetramer with four identical or near identical subunits. The Km estimates for G-1-P and ATP of the homogeneous preparation were 3.8e-5M and 1.8e-4M respectively. In addition to the endosperm ADPGlucose pyrophosphorylases, evidence is presented suggesting the presence of a different ADPGlucose pyrophosphorylase in the leaf tissue. Heat stability responses suggests that the enzyme is distinct from the endosperm ADPGlucose pyrophosphorylase but possibly similar or identical to the embryo ADPGlucose pyrophosphorylase.
Fuchs, Roy Lee (1977). Purification and characterization of ADPGlucose pyrophosphorylase A from maize endosperm. Texas A&M University. Texas A&M University. Libraries. Available electronically from
https : / /hdl .handle .net /1969 .1 /DISSERTATIONS -629895.