Abnormal lignins produced by the brown-midrib mutants of maize. II. Comparative studies on normal and brown-midrib-1 dimethylformamide lignins.
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Biomedical subjects
Publications and source records attributed to O E Nelson.
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Two phosphorylases have been found in the endosperm of Zea mays. Phosphorylase I is found through all stages of endosperm development and seed germination investigated. The other enzyme, phosphorylase II appears only at the stage of rapid starch biosynthesis and is not found during germination. At 22 days after pollination, the activity of phosphorylase II is 10 times that of phosphorylase I. These 2 phosphorylases are separable by column chromatography and behave differently in several respects.Phosphorylase I cannot utilize maltose as a primer while phosphorylase II does so readily. Furthermore, phosphorylase II can synthesize an amylose-like polymer from a "primer free" system after a lag phase.Phosphorylase II is inhibited severely at pH 5.8 by ATP, GTP, ADP, and GDP, and less drastically by UTP, CTP, UDP and CDP. Phosphorylase I is somewhat inhibited by purine nucleotides but not by pyrimidine nucleotides. In all cases, the inhibition is pH-dependent. Phosphorylase I is inhibited competitively by ATP while phosphorylase II is inhibited non-competitively.Phosphorylase II is markedly stimulated by 10 mm Mg(2+) and by 2 mm ethylenediamine tetraacetic acid while phosphorylase I is relatively little affected.
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The maize mutant shrunken-2 synthesizes only 25 to 30 percent as much starch as normal maize; it completely lacks adenosine diphosphate glucose pyrophosphorylase activity in both endosperm and embryo tissue. Identification of the mutant block indicates that the greater portion of starch in the endosperm of normal maize is synthesized by way of enzyme systems that utilize adenosine diphosphate glucose as a substrate, and that the latter is formed chiefly by adenosine diphosphate glucose pyrophosphorylase.
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