Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1976-8-23
pubmed:abstractText
Upon polyacrylamide gel electrophoresis, a soluble phenoloxidase from potatoes (var. Maritta) revealed 17 multiple forms with activity towards dopa and almost all other o-diphenols tested, but only 5 of the forms reacted with monophenols. Isoelectric focusing of the crude enzyme resulted in 2 main peaks with activity towards dopa, having isoelectric points at pH ranges 4.0-4.7 and 5.1-5.4: smaller amounts of the enzyme at higher pI values were also detected. When activity peaks were controlled by polyacrylamide gel electrophoresis, all bands previously detected by electrophoresis of the crude enzyme were recovered, but all peaks were electrophoretically heterogeneous. Gel chromatography of the crude enzyme showed different molecular forms. Their molecular weights indicated monomer, dimer, tetramer, octamer and polymer (at least hexadecamer) forms with a monomer molecular weight of about 36000.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0044-3026
pubmed:author
pubmed:issnType
Print
pubmed:day
7
pubmed:volume
157
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
221-7
pubmed:dateRevised
2000-12-18
pubmed:meshHeading
pubmed:year
1975
pubmed:articleTitle
Multiple forms of soluble monophenol, dihydroxyphenylalanine: oxygen-oxidoreductase (EC 1.14.18.1) from potato tubers (Solanum tuberosum).
pubmed:publicationType
Journal Article