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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2010-6-29
pubmed:abstractText
The enzyme putrescine hydroxycinnamoyl transferase (PHT) was purified 400-fold in 7.1% yield from tobacco (Nicotiana tabacum L. cv Xanthi) cell suspensions to a final specific activity of 45 nanokatal per milligram protein. The purification procedure involved conventional chromatography techniques (anion exchange chromatography, gel permeation, and hydroxylapatite chromatography) followed by chromatography on caffeoyl-cysteamine-Sepharose. This procedure led to considerable enrichment of a 50 kilodalton protein that could be further purified to near homogeneity by chromatofocalization (apparent isoelectric point = 8). PHT activity was repeatedly found associated with this protein, although approximately 66% of the enzymic activity was lost during chromatofocalization. Purified PHT exhibited the same properties as in the unpurified extract. It was not specific for putrescine and used other aliphatic diamines (mainly diaminopropane and cadaverine) as substrates. The most efficient phenolic substrate was caffeoyl-CoA, but cinnamoyl-, feruloyl-, sinapoyl-, and p-coumaroyl-CoA were also conjugated to putrescine, in decreasing order of activity. PHT could also use the artificial substrate p-fluorocinnamoyl-CoA.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:status
PubMed-not-MEDLINE
pubmed:month
Apr
pubmed:issn
0032-0889
pubmed:author
pubmed:issnType
Print
pubmed:volume
98
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1264-9
pubmed:dateRevised
2010-9-14
pubmed:year
1992
pubmed:articleTitle
Purification and Properties of Putrescine Hydroxycinnamoyl Transferase from Tobacco (Nicotiana tabacum) Cell Suspensions.
pubmed:affiliation
Laboratoire de Physiopathologie végétale, Institut National de la Recherche Agronomique, BV1540, 21034 Dijon Cedex France.
pubmed:publicationType
Journal Article