Range |
Table - link
|
Organism |
Bacteria Escherichia coli |
Reference |
Weickert MJ, Apostol I. High-fidelity translation of recombinant human hemoglobin in Escherichia coli. Appl Environ Microbiol. 1998 May64(5):1589-93PubMed ID9572921
|
Primary Source |
Neidhardt, F. C., and H. E. Umbarger. 1996. Modulation of chemical composition and other parameters of the cell by growth rate, p. 13–16. In F. C. Neidhardt, et al. (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. American Society for Microbiology, Washington, D.C. |
Method |
Coexpression of di-a-globin and b-globin in Escherichia coli in the presence of exogenous heme yielded high
levels of soluble, functional recombinant human hemoglobin (rHb1.1). |
Comments |
Table gives umol amino acid/gram of protein. Calculated from Primary Source assuming that 55% of protein dry weight is protein. For table giving amount of amino acid in cell dry weight see BNID 103344 |
Entered by |
Uri M |
ID |
104730 |