{"id":3788,"date":"2007-03-12T15:22:32","date_gmt":"2007-03-12T08:22:32","guid":{"rendered":"http:\/\/swallow-nest.com\/article\/2007\/03\/12\/distribution-of-neuraminidase-in-arthrobacter-and-its-purification-by-affinity-chromatography1-2\/"},"modified":"2007-03-12T15:22:32","modified_gmt":"2007-03-12T08:22:32","slug":"distribution-of-neuraminidase-in-arthrobacter-and-its-purification-by-affinity-chromatography1-2","status":"publish","type":"post","link":"https:\/\/indonesia-product.com\/news\/distribution-of-neuraminidase-in-arthrobacter-and-its-purification-by-affinity-chromatography1-2\/","title":{"rendered":"Distribution of Neuraminidase in Arthrobacter and Its Purification by Affinity Chromatography1"},"content":{"rendered":"<p><!--adsense--><br \/>\njb.oxfordjournals.org<br \/>\nYoshihiro UCHIDA,  Yoji TSUKADA and  Tsunetake SUGIMORI<\/p>\n<p>Kyoto Research Laboratories, Marukin Shoyu Co., Ltd. Uji, Kyoto 611<\/p>\n<p> Neuraminidase [sialidase, EC 3.2.1.18 [EC] ] was found to be widely distributed in bacteria belonging to Arthrobacter. Among these bacteria, Arthrobacter ureafaciens, A. oxydans, and A. aurescens produced relatively potent neuraminidase activities. For the production of this enzyme, not only colominic acid, a homopolymer of N-acetylneuraminic acid, but also N-acetylneuraminic acid, the reaction product of this enzyme, are effective as sources of carbon.<\/p>\n<p> An affinity adsorbent specific for neuraminidase was prepared by cross-linking colominic acid with soluble starch by means of epichlorohydrin. Neuraminidase from A. ureafaciens could be purified on this affinity column. The purified neuraminidase was shown to be free from protease, N-acetylneuraminic acid aldolase, phospholipase C, and glycosidases.<\/p>\n<p> Aminoff&#8217;s assay procedure for sialic acid was modified to avoid the centrifugation step. The modified procedure gave a higher molecular extinction coefficient.<\/p>\n<p>1A part of this paper was presented at the Annual Meeting of the Agricultural Chemical Society of Japan, Kyoto, April 1976.<\/p>\n","protected":false},"excerpt":{"rendered":"<p>jb.oxfordjournals.org Yoshihiro UCHIDA, Yoji TSUKADA and Tsunetake SUGIMORI Kyoto Research Laboratories, Marukin Shoyu Co., Ltd. Uji, Kyoto 611 Neuraminidase [sialidase, EC 3.2.1.18 [EC] ] was found to be widely distributed in bacteria belonging to Arthrobacter. Among these bacteria, Arthrobacter ureafaciens, A. oxydans, and A. aurescens produced relatively potent neuraminidase activities. For the production of this [&hellip;]<\/p>\n","protected":false},"author":5,"featured_media":0,"comment_status":"open","ping_status":"open","sticky":false,"template":"","format":"standard","meta":[],"categories":[413],"tags":[],"yoast_head":"<!-- This site is optimized with the Yoast SEO plugin v19.6 - https:\/\/yoast.com\/wordpress\/plugins\/seo\/ -->\n<title>Distribution of Neuraminidase in Arthrobacter and Its Purification by Affinity Chromatography1 - Directory of wholesale, manufacturers, distributors, importer and exporter in Indonesia<\/title>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"https:\/\/indonesia-product.com\/news\/distribution-of-neuraminidase-in-arthrobacter-and-its-purification-by-affinity-chromatography1-2\/\" \/>\n<meta property=\"og:locale\" content=\"en_US\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Distribution of Neuraminidase in Arthrobacter and Its Purification by Affinity Chromatography1 - Directory of wholesale, manufacturers, distributors, importer and exporter in Indonesia\" \/>\n<meta property=\"og:description\" content=\"jb.oxfordjournals.org Yoshihiro UCHIDA, Yoji TSUKADA and Tsunetake SUGIMORI Kyoto Research Laboratories, Marukin Shoyu Co., Ltd. Uji, Kyoto 611 Neuraminidase [sialidase, EC 3.2.1.18 [EC] ] was found to be widely distributed in bacteria belonging to Arthrobacter. Among these bacteria, Arthrobacter ureafaciens, A. oxydans, and A. aurescens produced relatively potent neuraminidase activities. 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