Methods in Molecular Biology • 16 Enzymes of Molecular Biology

(Nancy Kaufman) #1

Peptide Production 303



  1. Poncz, L. and Dearborn, D. G. (1983) The resistance to tryptic hydrolysis of
    peptide bonds adjacent to N,N-dimethyllysyl residues. J. Biol. Chem. 258,
    1844-1850.

  2. Bentz, H., Chang, R-J., Thompson, A. Y., Glaser, C. B., and Rosen, D. M.
    (1990) Amino acid sequence of bovine osteoinductive factor. J. Biol. Chem.
    265, 5024-5029.

  3. Tomasselli, A. G., Frank, R., and Schiltz, E. (1986) The complete primary
    structure of GTP:AMP phosphotransferase from beef heart mitochondria. FEBS
    Lett. 202, 303-307.

  4. Perides, G., Kuhn, S., Scherbarth, A., and Traub, P. (1987) Probing of the
    structural stability of vimentin and desmin-type intermediate filaments with
    Ca2÷-activated proteinase, thrombin and lysine-specific endoproteinase Lys-
    C. Eur. J. Cell Biol. 43, 450-458.

  5. Steffens, G. J, Gunzler, W. A., t3tting, F., Frankus, E., and Floh6, L. (1982)
    The complete amino acid sequence of low molecular weight urokinase from
    human urine. Hoppe-Seyler's Z. Physiol. Chem. 363, 1043-1058.

  6. Konigsberg, W., Goldstein, J., and Hill, R. J. (1963) The structure of human
    haemoglobin VII. The digestion of the 13 chain of human haemoglobin with
    pepsin. J. Biol. Chem. 238, 2028-2033.

  7. Price, N. C., Duncan, D., and McAlister, J. W. (1985) Inactivation of rabbit
    muscle phosphoglycerate mutase by limited proteolysis with thermolysin.
    Biochem. J. 229, 167-171.

  8. Eggerer, H. (1984) Hysteretic behaviour of citrate synthase. Site-directed lim-
    ited proteolysis. Eur. J. Biochem. 143, 205-212.

Free download pdf