Catalytically active monoamine oxidase type A from human liver expressed in Saccharomyces cerevisiae contains covalent FAD
- 31 December 1990
- journal article
- Published by Elsevier BV in Biochemical and Biophysical Research Communications
- Vol. 173 (3), 1205-1211
- https://doi.org/10.1016/s0006-291x(05)80914-3
Abstract
No abstract availableKeywords
This publication has 16 references indexed in Scilit:
- Primary structure of rat monoamine oxidase A deduced from cDNA and its expression in rat tissues.Agricultural and Biological Chemistry, 1990
- Biochemistry and genetics of monoamine oxidasePharmacology & Therapeutics, 1990
- Covalent cofactor binding to flavoenzymes requires specific effectorsJBIC Journal of Biological Inorganic Chemistry, 1989
- Molecular cloning of a cDNA for rat liver monoamine oxidase BBiochemical and Biophysical Research Communications, 1988
- Partial amino acid sequence analysis of human placenta monoamine oxidase A and bovine liver monoamine oxidase BBiochemical and Biophysical Research Communications, 1988
- Structural Features of Human Monoamine Oxidase A Elucidated from cDNA and Peptide SequencesJournal of Neurochemistry, 1988
- Expression of heterologous genes in Saccharomyces cerevisiae from vectors utilizing the glyceraldehyde-3-phosphate dehydrogenase gene promoterGene, 1984
- The Covalently‐Bound Flavin of Hepatic Monoamine OxidaseJBIC Journal of Biological Inorganic Chemistry, 1971
- The Covalently‐Bound Flavin of Hepatic Monoamine OxidaseJBIC Journal of Biological Inorganic Chemistry, 1971
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970