The state of the N-terminus of recombinant proteins: Determination of N-terminal methionine (formylated, acetylated, or free)
- 1 August 1987
- journal article
- research article
- Published by Elsevier in Analytical Biochemistry
- Vol. 165 (1), 59-69
- https://doi.org/10.1016/0003-2697(87)90201-6
Abstract
No abstract availableThis publication has 14 references indexed in Scilit:
- Purification and characterization of human interleukin‐1β expressed in recombinant Escherichia coliEuropean Journal of Biochemistry, 1986
- Separation of recombinant human interleukin-2 and methionyl interleukin-2 produced in EscherichiacoliBiochemical and Biophysical Research Communications, 1986
- Amino-terminal processing of proteins: hemoglobin South Florida, a variant with retention of initiator methionine and N alpha-acetylation.Proceedings of the National Academy of Sciences, 1985
- Methionine or not methionine at the beginning of a proteinBioEssays, 1985
- Synthesis of Escherichia coli carbomoylphosphate synthetase initiates at a UUG codonEuropean Journal of Biochemistry, 1985
- Sequence Determination of the Sendai Virus Fusion Protein GeneJournal of General Virology, 1985
- A new mass-spectrometric C-terminal sequencing technique finds a similarity between γ-interferon and α2-interferon and identifies a proteolytically clipped γ-interferon that retains full antiviral activityBiochemical Journal, 1983
- Amino acid sequence determination by g.l.c.-mass spectrometry of permethylated peptides. Optimization of the formation of chemical derivatives at the 2-10 nmol levelBiochemical Journal, 1983
- Efficient Bacterial Expression of Bovine and Porcine Growth HormonesDNA, 1983
- Accumulation of amino-terminally formylated tryptophan synthase in amplifying conditions.Agricultural and Biological Chemistry, 1983