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The optimum pH of phytolacain G was 7.5-8.0 at 37°C using casein as the substrate. The enzyme was strongly inhibited by iodoacetic acid and <i>p</i>-chloromercuribenzoic acid, but not by diisopropyl fluorophosphate or EDTA. These results indicated that phytolacain G was a cysteine protease, like phytolacain R. Nine sites of oxidized insulin B-chain were cleaved by phytolacain G during 20 h of hydrolysis. The six sites cleaved by phytolacain G were also cleaved by phytolacain R. The substrate specificity of phytolacain G was broad, but the preference for hydrophobic residues at the P<sub>2</sub> position was similar to the substrate specificity of papain. The amino-terminal sequence of phytolacain G was not identical with that of phytolacain R; however, the amino acid residues conserved in the papain family were also conserved in this enzyme.<br>"}],"abstractLicenseFlag":"disallow"}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1410001206473228929","@type":"Researcher","personIdentifier":[{"@type":"NRID","@value":"9000004163860"},{"@type":"NRID","@value":"9000253178713"},{"@type":"NRID","@value":"9000253173189"},{"@type":"NRID","@value":"9000020716933"},{"@type":"NRID","@value":"9000253174029"},{"@type":"NRID","@value":"9000255697874"},{"@type":"RESEARCHMAP","@value":"https://researchmap.jp/read0017879"}],"foaf:name":[{"@language":"en","@value":"UCHIKOBA Tetsuya"}],"jpcoar:affiliationName":[{"@language":"en","@value":"Department of Chemistry, Faculty of Science, Kagoshima 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Makoto"}],"jpcoar:affiliationName":[{"@language":"en","@value":"Department of Chemistry, Faculty of Science, Kagoshima University"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"09168451"},{"@type":"EISSN","@value":"13476947"},{"@type":"NDL_BIB_ID","@value":"000000151899"},{"@type":"ISSN","@value":"09168451"},{"@type":"LISSN","@value":"09168451"},{"@type":"NCID","@value":"AA10824164"}],"prism:publicationName":[{"@language":"en","@value":"Bioscience, Biotechnology, and Biochemistry"},{"@language":"ja","@value":"Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ"},{"@language":"en","@value":"Biosci. Biotechnol. Biochem."},{"@language":"en","@value":"Bioscience, Biotechnology, and Biochemistry"},{"@language":"ja","@value":"Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ"}],"dc:publisher":[{"@language":"en","@value":"Japan Society for Bioscience, Biotechnology, and Agrochemistry"},{"@language":"ja","@value":"公益社団法人 日本農芸化学会"}],"prism:publicationDate":"1998","prism:volume":"62","prism:number":"10","prism:startingPage":"2058","prism:endingPage":"2061"},"reviewed":"false","dcterms:accessRights":"http://purl.org/coar/access_right/c_abf2","url":[{"@id":"http://id.ndl.go.jp/bib/4666720"},{"@id":"https://ndlsearch.ndl.go.jp/books/R000000004-I4666720"},{"@id":"http://www.tandfonline.com/doi/pdf/10.1271/bbb.62.2058"}],"availableAt":"1998","foaf:topic":[{"@id":"https://cir.nii.ac.jp/all?q=%3Ci%3EPhytolacca%20americana%3C/i%3E","dc:title":"<i>Phytolacca americana</i>"},{"@id":"https://cir.nii.ac.jp/all?q=phytolaccaceae","dc:title":"phytolaccaceae"},{"@id":"https://cir.nii.ac.jp/all?q=pokeweed","dc:title":"pokeweed"},{"@id":"https://cir.nii.ac.jp/all?q=cysteine%20protease","dc:title":"cysteine protease"},{"@id":"https://cir.nii.ac.jp/all?q=phytolacain%20G","dc:title":"phytolacain G"}],"relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1360011144812007296","@type":"Article","relationType":["cites"],"jpcoar:relatedTitle":[{"@value":"CRYSTALLINE SOYBEAN TRYPSIN INHIBITOR"}]},{"@id":"https://cir.nii.ac.jp/crid/1360299768403756288","@type":"Article","relationType":["cites"],"jpcoar:relatedTitle":[{"@value":"Isolation and characterization of a protease from Phytolacca americana"}]},{"@id":"https://cir.nii.ac.jp/crid/1390001206475040384","@type":"Article","relationType":["cites"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Isolation of Phytolacain G and Its Inhibition Measured by Affinity Labeling."}]},{"@id":"https://cir.nii.ac.jp/crid/1570291226718925184","@type":"Article","relationType":["cites"]},{"@id":"https://cir.nii.ac.jp/crid/1570572699374631552","@type":"Article","relationType":["cites"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Performic acid oxidation."}]},{"@id":"https://cir.nii.ac.jp/crid/1570572699374632704","@type":"Article","relationType":["cites"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Roles of proteolytic enzymes in interactions of plants with other organism"}]},{"@id":"https://cir.nii.ac.jp/crid/1571135651728988672","@type":"Article","relationType":["cites"],"jpcoar:relatedTitle":[{"@language":"en","@value":"The Amino Acid Sequence of the Tryptic Peptides from Actinidin, a Proteolytic Enzyme from the Fruit of Actinidia chinensis"}]},{"@id":"https://cir.nii.ac.jp/crid/1571698601420003584","@type":"Article","relationType":["cites"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Purification and preliminary characterization of two asclepains from the latex of Asclepias syriaca L. 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