Linked Life Data

16657282

Source:http://linkedlifedata.com/resource/pubmed/id/16657282

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2010-6-29
pubmed:abstractText
The kinetic and spectral properties of peroxidases A and B from the dwarf tomato plant were compared. The absolute absorption spectra were essentially the same for peroxidases A and B and their derivatives. Peroxidases A and B had different pH optima with guaiacol as the hydrogen donor but essentially the same optimum when pyrogallol was the substrate. The substrate concentrations required for optimum activity were different not only for the different substrates but also for each isoenzyme. When pyrogallol was used as the substrate, peroxidases A and B were 80% active when assayed under conditions optimal for the other isoenzyme. When guaiacol was used as the substrate, peroxidase A was completely inactive when assayed under conditions optimal for peroxidase B. In this case the pH was not optimum and the H(2)O(2) concentration was inhibitory. Similarly, peroxidase B retained only 9% of its peroxidase activity toward guaiacol when assayed under conditions optimum for peroxidase A. In this case the pH was not optimum and the H(2)O(2) was limiting. A possible role for peroxidase isoenzymes is discussed.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:status
PubMed-not-MEDLINE
pubmed:month
Jan
pubmed:issn
0032-0889
pubmed:author
pubmed:issnType
Print
pubmed:volume
45
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
66-9
pubmed:dateRevised
2010-9-14
pubmed:year
1970
pubmed:articleTitle
Spectral similarities and kinetic differences of two tomato plant peroxidase isoenzymes.
pubmed:affiliation
Western Regional Research Laboratory, Agricultural Research Service, United States Department of Agriculture, Albany, California 94710.
pubmed:publicationType
Journal Article