West, B.L., Babbitt, P.C., Mendez, B. and Baxter, J.D. 1984. Creatine kinase protein sequence encoded by a cDNA made from Torpedo californica electric organ mRNA. Proc. Natl. Acad. Sci. USA. 81: 7007–7011.
Weir, M.P. and Sparks, J. 1987. Purification and renaturation of recombinant human interleukin-2. Biochem. J. 245: 5–91.
Sharma, S.K., Evans, D.B., Tomich, C.-S.C., Cornette, J.C. and Ulrich, R.G. 1987. Folding and activation of recombinant human prorenin. Biotech. Appld. Biochem. 9: 181–193.
Mitraki, A. and King, J. 1989. Protein folding intermediates and inclusion body formation. Bio/Technology 7: 690–697.
Marston, F.A.O. 1986. The purification of eukaryotic polypeptides synthesized in Escherichia coli. Biochem. J. 240: 1–12.
Schein, C.H. 1990. Solubility as a function of protein structure and solvent components. Bio/Technology 8: 308–317.
Schein, C.H. 1989. Production of soluble recombinant proteins in bacteria. Bio/Technology 7: 1141–1149.
Marston, F.A.O. 1987. The purification of eukaryotic polypeptides expressed in Escherichia coli 59–88. In: DNA Cloning: a Practical Approach (Vol. 3). Glover, D.M. (Ed.). IRL Press, Oxford, United Kingdom.
Lim, W.K., Smith-Somerville, H.E. and Hardman, J.K. 1989. Solubilization and renaturation of overexpressed aggregates of mutant tryptophan synthase α-subunits. Appl. Environ. Microbiol. 55: 1106–1111.
Hoess, A., Arthur, A.K., Wanner, G. and Fanning, E. 1988. Recovery of soluble, biologically active recombinant proteins from total bacterial lysates using ion exchange resins. Bio/Technology 6: 1214–1217.
Bolyard, M.G. and Lord, S.T. 1988. High-level expression of a functional human fibrinogen gamma chain in Escherichia coli. Gene 66: 183–192.
Nagai, K. and Thøgerson, H.C. Synthesis and sequence-specific proteolysis of hybrid proteins produced in Escherichia coli. Meth. in Enzymol. 153: 461–481.
Altman, J., Nilsson, B., Anderson, S. and Kuntz, I.D. 1990. Manuscript in preparation.
Babbitt, P.C., West, B.L., Kuntz, I.D. and Kenyon, G.L. 1988. Purification of the insoluble aggregate obtained from the expression of creatine kinase in E. coli yields greatly improved specific activity in the refolded protein. Biochem. 27: 3093.
Holmes, D.S. and Quigley, M. 1981. A rapid boiling method for the preparation of bacterial plasmids. Anal. Biochem. 114: 193–197.
Hartley, D.L. and Kane, J.F. 1988. Properties of inclusion bodies from recombinant Escherichia coli. Biochem. Soc. Trans. 16: 101–102.
Babbitt, P.C., West, B.L., Buechter, D.D., Chen, L.H., Kuntz, I.D. and Kenyon, G.L. Recovery of active creatine kinase refolded from inclusion bodies in Escherichia coli can be improved by removal of a contaminating protease. In: Protein Refolding. Georgiou, G. (Ed.). American Chemical Society, New York. In press.
Amann, E., Brosius, J. and Ptashne, M. 1983. Vectors bearing a hybrid trp-lac promoter useful for regulated expression of cloned genes in Escherichia coli. Gene 25: 167–178.
Meselson, M. and Yuan, R. 1968. DNA restriction enzyme from E. coli. Nature 217: 1110–1114.
Grossman, S.H., Pyle, J. and Steiner, R.J. 1981. Kinetic evidence for active monomers during the reassembly of denatured creatine kinase. Biochem. 20: 6122–6128.
Creighton, T.E. and Goldenberg, D.P. 1984. Folding pathway of a circular form of bovine pancreatic trypsin inhibitor. J. Mol. Biol. 179: 497–526.
Lowry, O.H., Rosebrough, N.J., Farr, A.L. and Randall, R.J. 1951. Protein measurement with the folin phenol reagent. J. Biol. Chem. 193: 265–275.
Bradford, M.M. 1976. A rapid and sensitive method for the quantita-tion of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Chem. 72: 248–254.
Tanzer, M.L. and Gilvarg, C.J. 1959. Creatine and creatine kinase measurement. J. Biol. Chem. 234: 3201–3204.
Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680–685.