Identification of the small subunit of ribulose 1,5-bisphosphate carboxylase as a product of wheat leaf cytoplasmic ribosomes.
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Biomedical subjects
Publications and source records attributed to H Roy.
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The influence of protein deficiency on the hepatotoxicity of carbon tetrachloride (CCl4) was investigated in a group of rhesus monkeys. Animals fed a protein-rich diet served as controls. The results indicate that protein-deficiency protects the liver against acute hepatotoxicity of this drug. The protective effect is abolished if the animals are administered phenobarbital prior to the administration of CCl4. The protective action is due to a reduction, in protein deficiency, of the endoplasmic reticulum associated enzymes involved in hepatotoxicity of CCl4. Repeated administration of CCl4, which induces hepatic regeneration, resulted in disappearance of fat from periportal cells in protein-deficient animals. The regenerating cells (because of their better enzyme system) acquire "nutritional autonomy" and are thus able to synthesize adequate amounts of lipoproteins for mobilization of liver triglycerides.
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The formation of a coupling factor.ADP complex is shown to be dependent on photoinduced electron transport, AMP, and P(i), and sensitive to arsenate and sulfate. The stability of the complex is unaffected by subsequent addition of arsenate, but is quite markedly sensitive to the addition of ADP. The data are discussed in relation to possible models of photophosphorylation, and in particular, to one in which coupling factor-bound, photosynthetically generated, ADP serves as a phosphoryl donor to substrate ADP.
The coupling factor of photophosphorylation, which carries out the terminal steps in the light-dependent synthesis of ATP in spinach chloroplasts, forms tight complexes with [(14)C]ADP in vitro. The bound [(14)C]ADP undergoes a transphosphorylation reaction to give [(14)C]AMP and [(14)C]ATP. The [(14)C]ATP remains tightly bound, and can be recovered conveniently only by denaturation of the enzyme nucleotide complex. If spinach membranes are illuminated in the presence of pyocyanine and [(3)H]AMP or [(32)P]P(i), the enzyme can be recovered as a tight complex with [(3)H]ADP or [(32)P]ADP. The evidence indicates that AMP is an earlier acceptor of phosphate than is ADP, in a light-driven phosphorylation reaction. It also suggests that AMP serves as a cofactor in photophosphorylation.
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