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Preparation and properties of antibody against pig kidney diamine oxidase

โœ Scribed by Arduino Oratore; Pietro Guerrieri; Amleto Ballini; Bruno Mondovi; Alessandro Finazzi Agro

Book ID
115910255
Publisher
Elsevier Science
Year
1979
Tongue
English
Weight
531 KB
Volume
104
Category
Article
ISSN
0014-5793

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Pig kidney diamine oxidase was purified to homogeneity. The reaction product of the cofactor with p-nitrophenylhydrazine (pNPH) was liberated with pronase treatment and purified. 1H NMR, uv/vis, and electrospray tandem mass spectroscopy revealed it to be a dipeptide with the sequence topaquinone-pNP

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An adduct with phenylhydrazine was formed with the purified pig kidney diamine oxidase and in parallel with the \(l\)-tyrosine decarboxylase from Streptococcus faecalis. The labeled enzymes were hydrolyzed by chemical hydrolysis and the adducts released by hydrolysis were isolated and identified fir