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pubmed:abstractText |
Small amounts of (+)-catechin (5 mg/kg body wt) administered intramuscularly to 8-day-old chicks raised the lysyl oxidase activity in aorta about 20%. (+)-Catechin had no effect on chicks that were copper-deficient. In the deficient chicks, (+)-catechin treatment prompted a substantially stronger increase in lysyl oxidase activity in response to CuSO4. The observed increments in lysyl oxidase activity in vivo were sensitive to inhibition by beta-aminopropionitrile (BAPN), suggesting that (+)-catechin was affecting the enzyme. (+)-Catechin in the assay medium partially inhibited lysyl oxidase activity. With excess copper ions present, (+)-catechin catalyzed a very strong release of volatile tritium from the substrate proteins. The release of tritium, indicative of lysyl oxidase activity, was not blocked by BAPN, suggesting that the activity in vitro was not enzyme catalyzed.
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