Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1987-5-22
pubmed:abstractText
The specific activity of K+-dependent p-NPPase (paranitrophenylphosphatase) from frog (Rana ridibunda) epidermis microsomal preparation was determined. The activity was proportional to time of incubation and protein concentrations under our assays conditions. Optimal phosphatase activity was at pH from 8 to 9 and over 35 degrees C. 10(-3) M ouabain inhibited 100% of the activity and the Ki was estimated about 5 X 10(-5) M. The Km for p-NPP was 3.8 mM and 2.1 for K+. The lectins GSI and GSII produced 80-90% of non-competitive inhibition of the activity. 50% of inhibition by GSI was obtained at 2 micrograms/ml. The Km for p-NPP did not change but the Vmax of activity was clearly reduced for both GSI and GSII lectins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0305-0491
pubmed:author
pubmed:issnType
Print
pubmed:volume
86
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
241-4
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Lectin inhibition and kinetics of microsomal K+-dependent p-nitrophenyl phosphatase of frog epidermis.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't