Linked Life Data

6362480

Source:http://linkedlifedata.com/resource/pubmed/id/6362480

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1984-2-14
pubmed:abstractText
Proteinase A was purified from commercial baker's yeast to homogeneity by using affinity chromatography. Simple and sensitive fluorometric assay procedures were developed for this enzyme, where Suc-Arg-Pro-Phe-His-Leu-Leu-Val-Tyr-4-methylcoumaryl-7-amide and dimethylcasein were used as synthetic substrate and protein substrate, respectively. Proteinase A cleaved the former substrate at the Leu-Val bond. The extent of the cleavage was monitored by measuring the amount of fluorescent 7-amino-4-methylcoumarine produced by the successive cleavage with an auxiliary enzyme, aminopeptidase M, or by measuring the fluorescence generated by the reaction of newly formed amino groups with fluorescamine. In the assay with the latter substrate, the amounts of newly formed amino groups were measured by the reaction with fluorescamine. The optimal pH of the reaction was 5.0 to 5.5. The methods were applied to the study of the effects of denaturing agents on the activity of proteinase A.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0003-2697
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
134
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
210-5
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Purification and fluorometric assay of proteinase A from yeast.
pubmed:publicationType
Journal Article