Linked Life Data

41378

Source:http://linkedlifedata.com/resource/pubmed/id/41378

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1980-1-28
pubmed:abstractText
Gel chromatography on Sepharose and on Sephadex was used to separate the soluble phenol oxidase in various potato juices into multiple molecular forms ranging from 36,000 to 800,000 daltons. Adjustment of potato juice from physiological pH (ca. 6) to pH 4.5 or to pH 7.8 resulted in the predominance of low-mol.-wt. (less than 150,000 daltons) or high-mol.-wt. (greater than 150,000 daltons) enzyme forms, respectively. This suggests association phenomena of subunits. In potato juice of physiological pH and in potato juice adjusted to pH 4.5, all enzyme forms exhibited both monophenol and o-diphenol oxidase activities (assayed at pH 6.0). In potato juice adjusted to pH 7.8 considerable loss of monophenol oxidase activity (assayed at pH 6.0) occurred. This suggests that o-diphenol oxidase is more alkali-stable than monophenol oxidase. The significance of these findings for enzyme purifications and for the in vivo action of the enzyme is discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0044-3026
pubmed:author
pubmed:issnType
Print
pubmed:volume
169
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
165-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
Multiple forms of soluble monophenol, dihydroxyphenylalanine: oxygen oxidoreductase (EC 1.14.18.1) from potato tubers (Solanum tuberosum). III. Influence of pH on the molecular weight distribution of enzyme activity in potato juice.
pubmed:publicationType
Journal Article, Comparative Study