{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,15]],"date-time":"2026-08-15T09:52:48Z","timestamp":1786787568444,"version":"build-2736575974"},"reference-count":0,"publisher":"National Academy of Sciences","issue":"15","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[1982,8]]},"abstract":"<jats:p>We have detected an endoglycosidase activity produced by Flavobacterium meningosepticum. This enzyme, named endo F, cleaves glycans of both the high-mannose and the complex type linked through asparagine to the protein backbone. The data indicate that cleavage occurs via hydrolysis of the glycosidic bond of the N,N'-diacetylchitobiose core structure adjacent to asparagine, similar to that due to endo H and endo D. Extreme variability was noted in the availability of this cleavage site among N-linked glycoproteins. Glycoproteins of retrovirus, lymphocytic choriomeningitis virus, Pichinde virus, and HLA-A and -B antigens were readily cleaved in the presence of nonionic detergent. Others, such as ovalbumin, fetuin, bromelain, ovomucoid, alpha 1-acid glycoprotein, immunoglobulin G, and influenza virus hemagglutinin became susceptible only after reduction and alkylation or when cleavage was performed in the presence of 1% 2-mercaptoethanol. Endo F should prove useful in the study of glycans and protein backbones as discrete entities and for defining the nature of the glycan-protein interface.<\/jats:p>","DOI":"10.1073\/pnas.79.15.4540","type":"journal-article","created":{"date-parts":[[2006,5,31]],"date-time":"2006-05-31T04:51:59Z","timestamp":1149051119000},"page":"4540-4544","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":430,"title":["endo-beta-N-acetylglucosaminidase F: endoglycosidase from Flavobacterium meningosepticum that cleaves both high-mannose and complex glycoproteins."],"prefix":"10.1073","volume":"79","author":[{"given":"J H","family":"Elder","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"S","family":"Alexander","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[1982,8]]},"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.79.15.4540","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,4,13]],"date-time":"2022-04-13T11:25:18Z","timestamp":1649849118000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.79.15.4540"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1982,8]]},"references-count":0,"journal-issue":{"issue":"15","published-print":{"date-parts":[[1982,8]]}},"alternative-id":["10.1073\/pnas.79.15.4540"],"URL":"https:\/\/doi.org\/10.1073\/pnas.79.15.4540","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[1982,8]]},"assertion":[{"value":"1982-08-01","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}