Linked Life Data

350873

Source:http://linkedlifedata.com/resource/pubmed/id/350873

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1978-8-28
pubmed:abstractText
Chitin synthetase was solubilized with digitonin from a particulate yeast fraction. The solubilized enzyme, which did not sediment at 200,000 X g and emerged after the void volume in a Sepharose 6B column, was active only after treatment with a protease. This confirms that chitin synthetase exists in the plasma membrane as a zymogen and that initiation of the chitin septum occurs by localized activation of the enzyme. By differential extraction with sodium cholate and digitonin, followed by chromatography on Sepharose 6B, a 20-fold purification of the enzyme was achieved with respect to the crude particles. The purified enzyme showed a requirement for a phospholipid; phosphatidylserine and lysophosphatidylserine were the best activators. Unsaturated fatty acids strongly inhibited synthetase activity, whereas their saturated counterparts were inert. The solubilized enzyme catalyzed the formation of insoluble chitin in the absence of added primer. The synthetic polysaccharide was examined by electron microscopy and found to consist of lozenge-shaped particles about 60 nm long and 10 nm wide.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
253
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4419-25
pubmed:dateRevised
2000-12-18
pubmed:meshHeading
pubmed:year
1978
pubmed:articleTitle
Solubilization and partial purification of yeast chitin synthetase. Confirmation of the zymogenic nature of the enzyme.
pubmed:publicationType
Journal Article