Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1977-3-21
pubmed:abstractText
The adsorption isotherms and the spreading tendency of microsomal nuclease (nucleate 3'-oligonucleotidohydrolase, EC 3.1.4.7) and bovine pancreatic ribonuclease (ribonucleate 3'-pyrimidino-oligonucleotidohydrolase, EC 3.1.4.22) in the presence of isopropyl alcohol as spreading agent have been determined using enzymes radioactively labelled by acetylation. In parallel, the concentration-surface pressure relations have been established. The enzymic activity of microsomal nuclease spread from isopropyl alcohol containing aqueous solutions was only a few percent of its activity in bulk, while the activity of the adsorbed enzyme was only slightly reduced. Adsorbed monolayers of RNAase were almost inactivated, while the spread monolayers in the presence of isopropyl alcohol became reactivated after exposure to the substrate for several hours. The exposure time for the reactivation decreases with increasing surface concentration.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
452
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
421-30
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1976
pubmed:articleTitle
Enzymic activity at interfaces. II. Enzymic activity of microsomal nuclease and bovine pancreatic ribonuclease at the air/water interface.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.