| pubmed-article:6404221 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6404221 | lifeskim:mentions | umls-concept:C0001554 | lld:lifeskim |
| pubmed-article:6404221 | lifeskim:mentions | umls-concept:C0085979 | lld:lifeskim |
| pubmed-article:6404221 | lifeskim:mentions | umls-concept:C0064545 | lld:lifeskim |
| pubmed-article:6404221 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:6404221 | pubmed:dateCreated | 1983-5-5 | lld:pubmed |
| pubmed-article:6404221 | pubmed:abstractText | The potential pharmacologic use of enzymes has long been considered. Practical applications, however, have been limited by the toxicity and allergic response to administered foreign proteins. A simple in vitro modification that allows the intraperitoneal administration of large doses of L-gulonolactone oxidase to guinea pigs is described. The enzyme is precipitated by guinea pig antisera and reacted with glutaraldehyde (0.125%). The product is comparatively nontoxic in guinea pigs. Administration of this enzyme enables guinea pigs to synthesize ascorbic acid. Success of this approach may depend on reinforcement by the bifunctional reagent of the enzyme-antibody complex. | lld:pubmed |
| pubmed-article:6404221 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6404221 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6404221 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:6404221 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6404221 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6404221 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6404221 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6404221 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6404221 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:6404221 | pubmed:issn | 0003-9861 | lld:pubmed |
| pubmed-article:6404221 | pubmed:author | pubmed-author:SatoP HPH | lld:pubmed |
| pubmed-article:6404221 | pubmed:author | pubmed-author:WaltonD MDM | lld:pubmed |
| pubmed-article:6404221 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6404221 | pubmed:volume | 221 | lld:pubmed |
| pubmed-article:6404221 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6404221 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6404221 | pubmed:pagination | 543-7 | lld:pubmed |
| pubmed-article:6404221 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:6404221 | pubmed:meshHeading | pubmed-meshheading:6404221-... | lld:pubmed |
| pubmed-article:6404221 | pubmed:meshHeading | pubmed-meshheading:6404221-... | lld:pubmed |
| pubmed-article:6404221 | pubmed:meshHeading | pubmed-meshheading:6404221-... | lld:pubmed |
| pubmed-article:6404221 | pubmed:meshHeading | pubmed-meshheading:6404221-... | lld:pubmed |
| pubmed-article:6404221 | pubmed:meshHeading | pubmed-meshheading:6404221-... | lld:pubmed |
| pubmed-article:6404221 | pubmed:meshHeading | pubmed-meshheading:6404221-... | lld:pubmed |
| pubmed-article:6404221 | pubmed:meshHeading | pubmed-meshheading:6404221-... | lld:pubmed |
| pubmed-article:6404221 | pubmed:meshHeading | pubmed-meshheading:6404221-... | lld:pubmed |
| pubmed-article:6404221 | pubmed:meshHeading | pubmed-meshheading:6404221-... | lld:pubmed |
| pubmed-article:6404221 | pubmed:meshHeading | pubmed-meshheading:6404221-... | lld:pubmed |
| pubmed-article:6404221 | pubmed:meshHeading | pubmed-meshheading:6404221-... | lld:pubmed |
| pubmed-article:6404221 | pubmed:year | 1983 | lld:pubmed |
| pubmed-article:6404221 | pubmed:articleTitle | Glutaraldehyde-reacted immunoprecipitates of L-gulonolactone oxidase are suitable for administration to guinea pigs. | lld:pubmed |
| pubmed-article:6404221 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6404221 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
