Protease-catalyzed synthesis of melanocyte-stimulating hormone (MSH) fragments
Journal of Protein Chemistry - 1983
Tóm tắt
In the present study on enzymatic peptide bond formation the proteosynthetic potential of several proteases was explored. Trypsin, α-chymotrypsin, papain, carboxypeptidase Y (CPD-Y), and thermolysin served as catalysts for the protease-controlled synthesis of some fragments of melanocyte-stimulating hormones. To obviate possible proteolytic cleavage of preexisting peptide bonds—a drawback often encountered during enzymatic peptide syntheses—several expedients leading to the target peptides were developed. The enzymatic procedure enabled under mild conditions the preparation of the desired peptides whose amino acid composition may give rise to severe complications during conventional syntheses.
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Anderson, G., and Luisi, P. L. (1979).Helv. Chim. Acta 62, 488–494.
Bennett, H. P. J., Lowry, P. J., McMartin, C., and Scott, A. P. (1974).Biochem. J. 141, 439–444.
Dayhoff, M. O. (1972).Atlas of Protein Sequence and Structure, Vol. 5, National Biomedical Research Foundation, Washington, D.C.
Döring, G., Kuhl, P., and Jakubke, H.-D. (1981).Monatsh. Chem. 112, 1165–1173.
Fruton, J. S. (1982).Adv. Enzymol. Relat. Areas Mol. Biol. 53, 239–306.
Hayashi, R., Bai, Y., and Hata, T. (1975).J. Biochem. 77, 69–79.
Hofmann, K., Woolner, M. E., Spuhler, G., and Schwartz, E. T. (1958).J. Am. Chem. Soc. 80, 1486–1489.
Hofmann, K., Finn, F. M., Limetti, M., Montibeller, J., and Zanetti, G. (1966).J. Am. Chem. Soc. 88, 3633–3639.
Isowa, Y., and Ichikawa, T. (1979).Bull. Chem. Soc. Jpn. 51, 796–800.
Jakubke, H.-D., and Kuhl, P. (1982).Pharmazie 33, 89–106.
Jost, R., Brambilla, E., Monti, J. C., and Luisi, P. L. (1980).Helv. Chim. Acta 63, 375–384.
Kemp, D. S. (1979). In Gross, E., and Meienhofer, J. (eds.),Peptides, Vol. 2, academic Press, New York, pp. 315–383.
Kullmann, W. (1980).J. Biol. Chem. 255, 8234–8238.
Kullmann, W. (1981).J. Biol. Chem. 256, 1301–1304.
Kullmann, W. (1982a).J. Org. Chem. 47, 5300–5303.
Kullmann, W. (1982b).Proc. Natl. Acad. Sci. USA 79, 2840–2844.
Milne, H. B., and Carpenter, F. H. (1968).J. Org. Chem. 33, 4476–4479.
Milne, H. B., and Kilday, W. (1965).J. Org. Chem. 30, 64–66.
Milne, H. B., Halver, J. E., Ho, D. S., and Mason, M. S. (1957).J. Am. Chem. Soc. 79, 637–639.
Morihara, K., and Oka, T. (1977).Biochem. J. 163, 531–542.
Nakanishi, S., Inouye, A., Kita, T., Nakamura, M., Chang, A. C. Y., Cohen, S. N., Numa, S. (1979).Nature 278, 423–427.
Oka, T., and Morihara, K. (1977).J. Biochem. (Tokyo)82, 1055–1062.
Oka, T., and Morihara, K. (1978).J. Biochem. (Tokyo)84, 1277–1283.
Otsuka, H., and Inouye, K. (1964).Bull. Chem. Soc. Jpn. 37, 1465–1471.
Schwyzer, R., and Li, C. H. (1958).Nature 182, 1669–1670.
Tanaka, A., Pickering, B. T., and Li, C. H. (1962).Arch. Biochem. Biophys. 99, 294–298.
Tsuzuki, H., Oka, T., and Morihara, K. (1980).J. Biochem. (Tokyo)88, 669–675.
Widmer, F., and Johansen, J. T. (1979).Carlsberg Res. Commun. 44, 37–46.
Widmer, F., Breddam, K., and Johansen, J. T. (1980).Carlsberg Res. Commun. 45, 453–463.
Yajima, H., and Kawatani, H. (1974). In Weinstein, B. (ed.),Chemistry and Biochemistry of Amino Acids, Peptides and Proteins, Vol. 2, Marcel Dekker,New York, pp. 39–143.
Yonemitsu, O., Mamada, T., and Kanaoka, Y. (1969).Tetrahedron Lett. 23, 1819–1820.