๐”– Bobbio Scriptorium
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The copper of porcine kidney diamine oxidase.

โœ Scribed by Frederick T. Greenaway; Zuwen He; John J. Hahn; Ning Xi; Yue Zou

Publisher
Elsevier Science
Year
1992
Tongue
English
Weight
104 KB
Volume
47
Category
Article
ISSN
0162-0134

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๐Ÿ“œ SIMILAR VOLUMES

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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