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Oxidation of epsilon-amino group of lysyl peptides by bovine serum amine oxidase.
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- Author(s): Oda O; Manabe T; Okuyama T
- Source:
Journal of biochemistry [J Biochem] 1981 Apr; Vol. 89 (4), pp. 1317-23.
- Publication Type:
Journal Article
- Language:
English
- Additional Information
- Source:
Publisher: Oxford University Press Country of Publication: England NLM ID: 0376600 Publication Model: Print Cited Medium: Print ISSN: 0021-924X (Print) Linking ISSN: 0021924X NLM ISO Abbreviation: J Biochem Subsets: MEDLINE
- Publication Information:
Publication: : Abingdon, UK : Oxford University Press
Original Publication: Tokyo : Japanese Biochemical Society
- Subject Terms:
- Abstract:
We examined whether bovine serum amine oxidase (BSAO) was able to oxidize lysyl peptides. Seven synthetic peptides, Z-Lys-Leu-OMe, Z-His-Lys-Leu-OMe, Z-Val-Leu-Gly-Lys-Leu-OMe, Ala-Ala-Lys, Ala-Lys-Ala, Phe-Lys, and Gly-Lys were incubated with BSAO at 37 degrees C for 4 days, and the extent of oxidation (H2O2 formation) was assayed by o-dianisidine method. The amino acid sequence of lysyl peptides affected the oxidation rate by BSAO. The rate of oxidation of Z-Lys-Leu-OMe was about fifty fold higher than that of Z-His-Lys-Leu-OMe. Z-Lys-Leu-OMe, the lysyl peptide most reactive with BSAO was analyzed by the 3-methyl-2-benzothiazolinone hydrochloride method, amino acid analysis, and the 2,4,6-trinitrobenzene sulfonic acid method. The production of aldehyde, a decrease in the lysine/leucine ratio, and a decrease in epsilon-amino group were confirmed. These results show that bovine serum amine oxidase is able to oxidize the epsilon-amino group of lysyl peptides.
- Accession Number:
0 (Aldehydes)
0 (Amines)
0 (Amino Acids)
0 (Dipeptides)
0 (Oligopeptides)
EC 1.4.3.21 (Amine Oxidase (Copper-Containing))
EC 1.5.- (Oxidoreductases Acting on CH-NH Group Donors)
K3Z4F929H6 (Lysine)
- Publication Date:
Date Created: 19810401 Date Completed: 19810915 Latest Revision: 20131121
- Publication Date:
20240829
- Accession Number:
6788757
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