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rdf:type |
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lifeskim:mentions |
|
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pubmed:issue |
1
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pubmed:dateCreated |
1989-6-26
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pubmed:databankReference |
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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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0378-1119
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
74
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
15-21
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
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pubmed:year |
1988
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pubmed:articleTitle |
Overproduction and purification of the M.HhaII methyltransferase from Haemophilus haemolyticus.
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pubmed:affiliation |
Department of Environmental Health Sciences, Johns Hopkins University School of Hygiene and Public Health, Baltimore, MD 21205.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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