{"title":"紫贻贝中与粘附有关的酚氧化酶的研究","authors":"Naohiro Maruyama, H. Etoh, K. Sakata, K. Ina","doi":"10.1271/BBB1961.55.2887","DOIUrl":null,"url":null,"abstract":"Assay for tyrosinase activity using L-dopa as the substrate. The enzyme activity was measured spectrophotometrically by the method of Pomerantz12) with a slight modification. The enzyme solution (0.2ml) was incubated at 25°C with 1.5ml of4mM D,L-dopa in 0.1m sodium phosphate buffer, pH 6.5, containing 0.9% (w/v) NaCl. The conversion of L-dopa to dopachrome was followed by monitoring the increase of absorbance at","PeriodicalId":7729,"journal":{"name":"Agricultural and biological chemistry","volume":"9 5 1","pages":"2887-2889"},"PeriodicalIF":0.0000,"publicationDate":"1991-11-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"9","resultStr":"{\"title\":\"Studies on phenoloxidase from Mytilus edulis associated with adhesion\",\"authors\":\"Naohiro Maruyama, H. Etoh, K. Sakata, K. Ina\",\"doi\":\"10.1271/BBB1961.55.2887\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Assay for tyrosinase activity using L-dopa as the substrate. The enzyme activity was measured spectrophotometrically by the method of Pomerantz12) with a slight modification. The enzyme solution (0.2ml) was incubated at 25°C with 1.5ml of4mM D,L-dopa in 0.1m sodium phosphate buffer, pH 6.5, containing 0.9% (w/v) NaCl. The conversion of L-dopa to dopachrome was followed by monitoring the increase of absorbance at\",\"PeriodicalId\":7729,\"journal\":{\"name\":\"Agricultural and biological chemistry\",\"volume\":\"9 5 1\",\"pages\":\"2887-2889\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1991-11-23\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"9\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Agricultural and biological chemistry\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1271/BBB1961.55.2887\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Agricultural and biological chemistry","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1271/BBB1961.55.2887","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Studies on phenoloxidase from Mytilus edulis associated with adhesion
Assay for tyrosinase activity using L-dopa as the substrate. The enzyme activity was measured spectrophotometrically by the method of Pomerantz12) with a slight modification. The enzyme solution (0.2ml) was incubated at 25°C with 1.5ml of4mM D,L-dopa in 0.1m sodium phosphate buffer, pH 6.5, containing 0.9% (w/v) NaCl. The conversion of L-dopa to dopachrome was followed by monitoring the increase of absorbance at