| pubmed-article:6812050 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6812050 | lifeskim:mentions | umls-concept:C0086300 | lld:lifeskim |
| pubmed-article:6812050 | lifeskim:mentions | umls-concept:C0205242 | lld:lifeskim |
| pubmed-article:6812050 | lifeskim:mentions | umls-concept:C0017968 | lld:lifeskim |
| pubmed-article:6812050 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:6812050 | lifeskim:mentions | umls-concept:C0014162 | lld:lifeskim |
| pubmed-article:6812050 | lifeskim:mentions | umls-concept:C0014158 | lld:lifeskim |
| pubmed-article:6812050 | pubmed:issue | 15 | lld:pubmed |
| pubmed-article:6812050 | pubmed:dateCreated | 1982-12-2 | lld:pubmed |
| pubmed-article:6812050 | pubmed:abstractText | 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. | lld:pubmed |
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| pubmed-article:6812050 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:6812050 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:6812050 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6812050 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:6812050 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:6812050 | pubmed:author | pubmed-author:AlexanderSS | lld:pubmed |
| pubmed-article:6812050 | pubmed:author | pubmed-author:ElderJ HJH | lld:pubmed |
| pubmed-article:6812050 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6812050 | pubmed:volume | 79 | lld:pubmed |
| pubmed-article:6812050 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6812050 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6812050 | pubmed:pagination | 4540-4 | lld:pubmed |
| pubmed-article:6812050 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:6812050 | pubmed:meshHeading | pubmed-meshheading:6812050-... | lld:pubmed |
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| pubmed-article:6812050 | pubmed:meshHeading | pubmed-meshheading:6812050-... | lld:pubmed |
| pubmed-article:6812050 | pubmed:year | 1982 | lld:pubmed |
| pubmed-article:6812050 | pubmed:articleTitle | endo-beta-N-acetylglucosaminidase F: endoglycosidase from Flavobacterium meningosepticum that cleaves both high-mannose and complex glycoproteins. | lld:pubmed |
| pubmed-article:6812050 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6812050 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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