pubmed-article:3248721 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:3248721 | lifeskim:mentions | umls-concept:C0317567 | lld:lifeskim |
pubmed-article:3248721 | lifeskim:mentions | umls-concept:C0025831 | lld:lifeskim |
pubmed-article:3248721 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
pubmed-article:3248721 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:3248721 | pubmed:dateCreated | 1989-6-26 | lld:pubmed |
pubmed-article:3248721 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3248721 | pubmed:abstractText | The HhaII methyltransferase gene from Haemophilus haemolyticus was subcloned in an expression vector under control of the hybrid trp-lac promoter. Induction with isopropyl-beta-D-thiogalactopyranoside results in overproduction of the methyltransferase to about 3% of total cellular protein. The methyltransferase was purified to near electrophoretic homogeneity by phosphocellulose, DEAE, and gel chromatography. Its monomer Mr by sodium dodecyl sulfate-polyacrylamide gel electrophoresis is 25 kDa, in good agreement with that predicted from the nucleotide sequence. Crystals of the methyltransferase were obtained in the presence of a two-fold molar excess of the duplex oligodeoxynucleotide substrate 5'd-GGACTCC.CCTGAGG. | lld:pubmed |
pubmed-article:3248721 | pubmed:language | eng | lld:pubmed |
pubmed-article:3248721 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3248721 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:3248721 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3248721 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3248721 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3248721 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3248721 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3248721 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:3248721 | pubmed:month | Dec | lld:pubmed |
pubmed-article:3248721 | pubmed:issn | 0378-1119 | lld:pubmed |
pubmed-article:3248721 | pubmed:author | pubmed-author:SmithH OHO | lld:pubmed |
pubmed-article:3248721 | pubmed:author | pubmed-author:Chandrasegara... | lld:pubmed |
pubmed-article:3248721 | pubmed:author | pubmed-author:WuL PLP | lld:pubmed |
pubmed-article:3248721 | pubmed:author | pubmed-author:WALNEP RPR | lld:pubmed |
pubmed-article:3248721 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:3248721 | pubmed:day | 25 | lld:pubmed |
pubmed-article:3248721 | pubmed:volume | 74 | lld:pubmed |
pubmed-article:3248721 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:3248721 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:3248721 | pubmed:pagination | 15-21 | lld:pubmed |
pubmed-article:3248721 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:3248721 | pubmed:meshHeading | pubmed-meshheading:3248721-... | lld:pubmed |
pubmed-article:3248721 | pubmed:meshHeading | pubmed-meshheading:3248721-... | lld:pubmed |
pubmed-article:3248721 | pubmed:meshHeading | pubmed-meshheading:3248721-... | lld:pubmed |
pubmed-article:3248721 | pubmed:meshHeading | pubmed-meshheading:3248721-... | lld:pubmed |
pubmed-article:3248721 | pubmed:meshHeading | pubmed-meshheading:3248721-... | lld:pubmed |
pubmed-article:3248721 | pubmed:meshHeading | pubmed-meshheading:3248721-... | lld:pubmed |
pubmed-article:3248721 | pubmed:meshHeading | pubmed-meshheading:3248721-... | lld:pubmed |
pubmed-article:3248721 | pubmed:meshHeading | pubmed-meshheading:3248721-... | lld:pubmed |
pubmed-article:3248721 | pubmed:meshHeading | pubmed-meshheading:3248721-... | lld:pubmed |
pubmed-article:3248721 | pubmed:year | 1988 | lld:pubmed |
pubmed-article:3248721 | pubmed:articleTitle | Overproduction and purification of the M.HhaII methyltransferase from Haemophilus haemolyticus. | lld:pubmed |
pubmed-article:3248721 | pubmed:affiliation | Department of Environmental Health Sciences, Johns Hopkins University School of Hygiene and Public Health, Baltimore, MD 21205. | lld:pubmed |
pubmed-article:3248721 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:3248721 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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