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Primary structures for a mammalian cellular and serum copper amine oxidase
D Mu1, K F Medzihradszky, G W Adams
1Department of Chemistry, University of California, Berkeley 94720.
The Journal of Biological Chemistry
|April 1, 1994
Summary
Researchers identified the human kidney amiloride-binding protein as diamine oxidase. This study provides the first primary sequences for mammalian copper amine oxidases, revealing conserved histidine residues likely involved in copper binding.
Area of Science:
- Biochemistry
- Molecular Biology
- Enzymology
Background:
- The active site peptide of bovine serum amine oxidase shows homology to human kidney amiloride-binding protein.
- Peptides from bovine serum amine oxidase and porcine kidney diamine oxidase are contained within the human kidney amiloride-binding protein sequence.
Purpose of the Study:
- To determine if the human kidney amiloride-binding protein encodes a diamine oxidase.
- To obtain the primary sequences for mammalian cellular and serum copper amine oxidases.
Main Methods:
- Peptide sequencing and homology analysis.
- Amiloride binding assays.
- Polymerase chain reaction (PCR) amplification of cDNA.
- cDNA library screening.
Main Results:
- The human kidney amiloride-binding protein sequence contains peptides from bovine serum amine oxidase and porcine kidney diamine oxidase.
- Amiloride binding constants were determined for bovine serum amine oxidase and porcine kidney diamine oxidase.
- Full-length cDNA for bovine serum amine oxidase was obtained, providing its primary sequence.
- Three conserved histidine residues were identified in mammalian copper amine oxidases.
Conclusions:
- The human kidney amiloride-binding protein cDNA encodes human kidney diamine oxidase.
- This research presents the first primary sequences for mammalian cellular and serum copper amine oxidases.
- Conserved histidine residues are likely copper ligands in these enzymes.