Linked Life Data

19129636

Source:http://linkedlifedata.com/resource/pubmed/id/19129636

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2009-1-23
pubmed:abstractText
Membrane-bound glucono-delta-lactonase (MGL) was purified to homogeneity from the membrane fraction of Gluconobacter oxydans IFO 3244. After solubilization with 1 M CaCl2, MGL was purified in the presence of Ca2+ and detergent. A single band corresponding to 60 kDa appeared in SDS-PAGE. The molecular weight of MGL was judged to be 120 k. Differently from cytoplasmic lactonases, MGL showed optimum pH in an acidic range of 5-5.5. It was highly sensitive to metal-chelating agents such as EDTA, and the lost MGL activity was restored to the original level by the addition of divalent cations such as Ca2+ or Mg2+. The purified MGL was strictly dependent on Ca2+ and underwent rapid denaturing precipitation on Ca2+ depletion even in the presence of detergent. This communication can be the first one dealing with the solubilization, purification and properties of MGL.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1347-6947
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
73
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
241-4
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Solubilization, purification, and properties of membrane-bound D-glucono-delta-lactone hydrolase from Gluconobacter oxydans.
pubmed:affiliation
Department of Chemical and Biological Engineering, Ube National College of Technology. emiko@ube-k.ac.jp
pubmed:publicationType
Journal Article