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| Creator | Title | Description | Subject | Date | ||
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Baehr, Wolfgang | Isolation and characterization of cGMP phosphodiesterase from bovine rod outer segments | A simple purification method has been developed for isolation of bovine cGMP phosphodiesterase from photoreceptor rod outer segments. The enzyme is peripherally membrane bound in its native state and is present in relatively high concentrations. In the bovine photoreceptors its molar ratio to rhodop... | Enzyme Activation; Macromolecular Substances; Trypsin/pharmacology | 1979 |
| 2 |
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Fu, Yingbin | Mechanism of reductive activation of potato tuber ADP-glucose pyrophosphorylase. | The potato tuber (Solanum tuberosum L.) ADP-glucose pyrophosphorylase activity is activated by a incubation with ADP-glucose and dithiothreitol or by ATP, glucose- 1-phosphate, Ca2+, and dithiothreitol. The activation was accompanied by the appearance of new sulfhydryl groups as determined with 5, 5... | Glucosephosphates; Enzyme Activation; Adenosine Triphosphate | 1998 |
| 3 |
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Poulter, Charles Dale | Yeast squalene synthase. A mechanism for addition of substrates and activation by NADPH | Squalene synthase catalyzes the condensation of two molecules of farnesyl diphosphate (FPP) to give presqualene diphosphate (PSPP) and the subsequent reductive rearrangement of PSPP to squalene. Previous studies of the mechanism of addition of FPP to the enzyme have led to conflicting interpretation... | Enzyme Activation; Sesquiterpenes; Kinetics | 1993-04-15 |
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