| pubmed-article:2429588 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2429588 | lifeskim:mentions | umls-concept:C0007367 | lld:lifeskim |
| pubmed-article:2429588 | lifeskim:mentions | umls-concept:C0487602 | lld:lifeskim |
| pubmed-article:2429588 | lifeskim:mentions | umls-concept:C0456387 | lld:lifeskim |
| pubmed-article:2429588 | lifeskim:mentions | umls-concept:C0205173 | lld:lifeskim |
| pubmed-article:2429588 | lifeskim:mentions | umls-concept:C0972569 | lld:lifeskim |
| pubmed-article:2429588 | lifeskim:mentions | umls-concept:C0071499 | lld:lifeskim |
| pubmed-article:2429588 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:2429588 | pubmed:dateCreated | 1986-11-14 | lld:pubmed |
| pubmed-article:2429588 | pubmed:abstractText | Mycobacteria produce two classes of catalase, designated T and M. Only the T-catalase also has a peroxidase-like function. When a 3,3'-diaminobenzidine (DAB) peroxidase stain was applied to polyacrylamide gel electrophoresis gels, followed by a ferricyanide negative stain for catalase, isoenzymes of T-catalase appeared as dark bands within a zone of clearing in the green background; the M-catalase appeared only as a clear zone. Heated and unheated preparations could be used to demonstrate the presence of comigrating bands of M and T. The application of the ferricyanide stain after the DAB stain of T-catalase resulted in marked intensification of the positive bands of T-catalase due to nonenzymatic, peroxide-independent reduction of the ferricyanide by the DAB product. | lld:pubmed |
| pubmed-article:2429588 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2429588 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2429588 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2429588 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:2429588 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2429588 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2429588 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:2429588 | pubmed:issn | 0003-2697 | lld:pubmed |
| pubmed-article:2429588 | pubmed:author | pubmed-author:WayneL GLG | lld:pubmed |
| pubmed-article:2429588 | pubmed:author | pubmed-author:DiazG AGA | lld:pubmed |
| pubmed-article:2429588 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2429588 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:2429588 | pubmed:volume | 157 | lld:pubmed |
| pubmed-article:2429588 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2429588 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2429588 | pubmed:pagination | 89-92 | lld:pubmed |
| pubmed-article:2429588 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:2429588 | pubmed:meshHeading | pubmed-meshheading:2429588-... | lld:pubmed |
| pubmed-article:2429588 | pubmed:meshHeading | pubmed-meshheading:2429588-... | lld:pubmed |
| pubmed-article:2429588 | pubmed:meshHeading | pubmed-meshheading:2429588-... | lld:pubmed |
| pubmed-article:2429588 | pubmed:meshHeading | pubmed-meshheading:2429588-... | lld:pubmed |
| pubmed-article:2429588 | pubmed:meshHeading | pubmed-meshheading:2429588-... | lld:pubmed |
| pubmed-article:2429588 | pubmed:meshHeading | pubmed-meshheading:2429588-... | lld:pubmed |
| pubmed-article:2429588 | pubmed:year | 1986 | lld:pubmed |
| pubmed-article:2429588 | pubmed:articleTitle | A double staining method for differentiating between two classes of mycobacterial catalase in polyacrylamide electrophoresis gels. | lld:pubmed |
| pubmed-article:2429588 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2429588 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:2429588 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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