کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1926785 | 1536476 | 2008 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Tyramine oxidation by copper/TPQ amine oxidase and peroxidase from Euphorbia characias latex
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Tyramine oxidation by copper/TPQ amine oxidase and peroxidase from Euphorbia characias latex Tyramine oxidation by copper/TPQ amine oxidase and peroxidase from Euphorbia characias latex](/preview/png/1926785.png)
چکیده انگلیسی
Tyramine, an important plant intermediate, was found to be a substrate for two proteins, a copper amine oxidase and a peroxidase from Euphorbia characias latex. The oxidation of tyramine took place by two different mechanisms: oxidative deamination to p-hydroxyphenylacetaldehyde by the amine oxidase and formation of di-tyramine by the peroxidase. The di-tyramine was further oxidized at the two amino groups by the amino oxidase, whereas p-hydroxyphenylacetaldehyde was transformed to di-p-hydroxyphenylacetaldehyde by the peroxidase. Data obtained in this study indicate a new interesting scenario in the metabolism of tyramine.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Archives of Biochemistry and Biophysics - Volume 475, Issue 1, 1 July 2008, Pages 18–24
Journal: Archives of Biochemistry and Biophysics - Volume 475, Issue 1, 1 July 2008, Pages 18–24
نویسندگان
Anna Mura, Francesca Pintus, Antonella Fais, Simona Porcu, Marcella Corda, Delia Spanò, Rosaria Medda, Giovanni Floris,