Linked Life Data

132193

Source:http://linkedlifedata.com/resource/pubmed/id/132193

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1976-9-1
pubmed:abstractText
A soluble purified form of Micrococcus lysodeikticus ATPase (form BAT, from strain B, active, trypsin-stimulated) was stimulated 100% by trypsin and this stimulation was inhibited by preincubation of the protease with phenyl methyl sulphonylfluoride. This form of the enzyme was also stimulated 125-150% by filtration on Sephadex G-200. Analysis by sodium dodecyl sulphate-gel electrophoresis showed that stimulation of this form of M. lysodeikticus ATPase was always accompanied by the disappearance of a subunit of mol. wt. 25000 (epsilon subunit). It suggests that this subunit is the natural inhibitor of M. lysodeikticus ATPase. In the case of ATPase stimulation by trypsin, a partial and limited degradation of the alpha subunit was also observed. The interaction between the epsilon subunit and the rest of the ATPase complex was reversibly affected by pH, suggesting its non-covalent nature.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
436
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
183-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1976
pubmed:articleTitle
Micrococcus lysodeikticus membrane ATPase. Effect of trypsin on stimulation of a purified form of the enzyme and idenfification of its natural inhibitor.
pubmed:publicationType
Journal Article