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Homocitrate synthase from yeast.
Homocitrate synthase activity has been partially purified from yeast and was sensitive to inhibition by lysine both in vivo and in vitro only at high concentrations ofLysine. Expand
The removal of the bound ADP of F-actin.
It is suggested that the bound ADP of F-actin is not involved in the physiologically important properties of F -actin, namely, the activation of the ATPase activity of myOSin and superprecipitation with myosin in the presence of ATP. Expand
Myosin in newborn rabbits.
Accumulation of α-ketoglutaric acid in yeast mutants requiring lysine☆
Accumulation of a-ketoglutaric acid in two nonallelic yeast mutants (Ly7 and Ly4) requiring lysine has been demonstrated, and data suggest that there are two different enzymic steps to convert homocitrate to homisocitrates. Expand
Preparation and properties of porcine parotid butyrylcholinesterase.
Substrate specificity and inhibitor studies indicated that the enzyme is a butyrylcholinesterase of the type described in porcine serum and colostrum, and over a broad range of acetylcholine concentrations, the enzyme follows MichaelisMenten kinetics. Expand
Synthesis and absolute configuration of the isomers of homoisocitric acid (1-hydroxy-1,2,4-butanetricarboxylic acid) and the stereochemistry of lysine biosynthesis.
Homoisocitric dehydrogenase from yeast.
Purified homoisocitric dehydrogenase did not catalyze the oxidation of ethanol, isocitrate, malate, or glutamate in the presence of the appropriate cofactors. Expand
Control of lysine biosynthesis in yeast.
The site sensitive to inhibition at low concentrations of lysine is after α-aminoadipate on the pathway, and no evidence was obtained to demonstrate a branch point in the pathway. Expand
Fluorometric assay of malic acid and substituted derivatives.
The fluorometric assay was shown to be useful over a wide range of concentrations, and is sensitive enough to be used for less than microgram quantities of α-substituted malic acids. Expand
Accumulation of alpha-ketoglutaric acid in yeast mutants requiring lysine.