Purification and characterization of peptidylglycine alpha-amidating monooxygenase from bovine neurointermediate pituitary.
Open Access
- 1 February 1986
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 261 (4) , 1815-1822
- https://doi.org/10.1016/s0021-9258(17)36013-1
Abstract
No abstract availableThis publication has 25 references indexed in Scilit:
- Characterization of a peptide alpha-amidation activity in human plasma and tissuesMetabolism, 1985
- Glycine-directed peptide amidation: presence in rat brain of two enzymes that convert p-Glu-His-Pro-Gly-OH into p-Glu-His-Pro-NH2 (thyrotropin-releasing hormone).Proceedings of the National Academy of Sciences, 1984
- C‐terminal amidation of neuropeptidesFEBS Letters, 1984
- Microtubule assembly using the microtubule‐associated protein MAP‐2 prepared in defined states of phosphorylation with protein kinase and phosphataseEuropean Journal of Biochemistry, 1983
- Bovine intermediate pituitary α-amidation enzyme: Preliminary characterizationPeptides, 1983
- Substrate specificity of an amidating enzyme in porcine pituitaryBiochemical and Biophysical Research Communications, 1983
- Formation of the COOH‐terminal amide group of thyrotropin‐releasing‐factorFEBS Letters, 1983
- Mechanism of C-terminal amide formation by pituitary enzymesNature, 1982
- DISTRIBUTION OF ASCORBIC ACID, METABOLITES AND ANALOGUES IN MAN AND ANIMALSAnnals of the New York Academy of Sciences, 1975
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970