Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1989-11-6
pubmed:abstractText
Cu-Amine oxidases (amine oxygen oxidoreductase deaminating, copper containing E.C. 1.4.3.6.) are found in all forms of life (1). They catalyze the following general reaction: R-CH2-NH2 + O2 + H2O----R-CHO + NH3 + H2O2. Cu-amine oxidases (Cu-AOs) have been extracted from different leguminosae: Pisum sativum (2-3), Lathyrus sativus (4), Lens esculenta (5), Vicia faba (6), Cicer arietinum (7), Glycine max (8) but not from Phaseolus vulgaris. Palavan and Galston (9), in a study of polyamine biosynthesis during developmental stages of Phaseolus vulgaris, did not detect diamine or polyamine oxidase activity in Phaseolus. The present paper describes the purification of Phaseolus vulgaris seedlings amine oxidase (PhSAO) and also compares the properties of this enzyme to the Lathyrus cicera enzyme (LcSAO), obtained with the same method of purification.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0032-7484
pubmed:author
pubmed:issnType
Print
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
95-112
pubmed:dateRevised
2005-11-17
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Amine oxidase from Lathyrus cicera and Phaseolus vulgaris: purification and properties.
pubmed:affiliation
Istituto di Chimica Biologica, Università di Cagliari, Italy.
pubmed:publicationType
Journal Article