Sub-microgram per gram concentrations of mercury in orchard leaves determined by isotope dilution and spark-source mass spectrometry.
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Biomedical subjects
Publications and source records attributed to R Alvarez.
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Barley seed (Hordeum vulgare L.) homogenates contain an apparent enzymatic activity which catalyzes the synthesis of adenosine 5'-phosphorofluoridate from magnesium-adenosine 5'-triphosphate and sodium fluoride. Formation of this compound may interfere with some adenyl cyclase assays which use fluoride as a component of the incubation medium. Neither adenyl cyclase activity nor endogenous adenosine 3': 5'-monophosphate was detected in barley seed homogenates or extracts.
Barley seeds (Hordeum vulgare L. cv. Himalaya) contain an enzymatic activity which catalyzes the hydrolysis of adenosine cyclic 3': 5'-monophosphate and adenosine cyclic 2': 3'-monophosphate. A large portion of the enzymatic activity is present in the dry seed, existing in both soluble and particulate form. Secretion of the soluble phosphodiesterase from embryoless seeds is enhanced by gibberellic acid and inhibited by abscisic acid, dinitrophenol, and cycloheximide. Attempts to isolate or detect a phosphodiesterase which specifically hydrolyzes adenosine cyclic 3': 5'-monophosphate were unsuccessful. Inhibition experiments indicate that probably one enzyme is involved in the hydrolysis of both of these substrates.
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