Summary
Two fragments (Mr =38,000 and 14,000)derived from limited trypsin treatment of pig kidney Dopa decarboxylase have been separated in denaturing conditions. The PLP-binding site has been located on the larger fragment. Results of sequence analysis by automated Edman degradation of the intact enzyme compared with those of the two fragments indicate that the cleavage takes place at about one-third from the COOH-terminal. A 50 residue NH2-terminal of the smaller fragment has been determined.
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References
Borri Voltattorni, C., Minelli, A., Vecchini, P., Fiori, A. and Turano, C. (1979) Eur. J. Biochem., 93, 181–188.
Bossa, F., Martini, F., Barra, D., Borri Voltattorni, C., Minelli, A. and Turano, C. (1977) Biochem. Biophys. Res. Comm., 18, 177–183.
Eveleth, D. D., Gietz, R. D., Spencer, C. A., Nargang, F. E., Hodgetts, R. B. and Marsh, J. L. (1986) Embo J., 5, 2663–2672.
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© 1987 Birkhäuser Verlag Basel
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Dominici, P., Tancini, B., Simmaco, M., Barra, D., Bossa, F., Voltattorni, C.B. (1987). Proteolytic Cleavage of Pig Kidney Dopa Decarboxylase. In: Korpela, T.K., Christen, P. (eds) Biochemistry of Vitamin B6 . Birkhäuser Congress Reports. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-9308-4_35
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DOI: https://doi.org/10.1007/978-3-0348-9308-4_35
Publisher Name: Birkhäuser, Basel
Print ISBN: 978-3-0348-9989-5
Online ISBN: 978-3-0348-9308-4
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