The thiol proteinases from the latex of carica papaya l.: II. the primary structure of proteinase il;Die thiol-proteinasen aus dem milchsaft von carica papaya l. II. die primärstruktur der proteinase

Biological Chemistry Hoppe-Seyler

Volumn 369, Issue 2, 1988, Pages 741-754

  Dubois, Thierry ^a   Kleinschmidt, Traute ^b   Schnek, Arthur G ^b   Looze, Yvan ^b   Braunitzer, Gerhard ^c  

^a UNIVERSITÉ LIBRE DE BRUXELLES   (Belgium)

^b Max Planck Institut für Biochemie Abteilung Proteinchemie Martinsried bei München ^*  (Germany)

^c MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

Carica papaya; cysteine proteinases; primary structure; proteases; Proteinase

Indexed keywords

CARICAIN; CYSTEINE PROTEINASE; DISULFIDE; LATEX; PEPTIDE FRAGMENT; PEPTIDE HYDROLASE; VEGETABLE PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; COMPARATIVE STUDY; ENZYMOLOGY; MOLECULAR GENETICS; PLANT; SEQUENCE HOMOLOGY; TREE;

AMINO ACID SEQUENCE; CYSTEINE ENDOPEPTIDASES; DISULFIDES; LATEX; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PEPTIDE HYDROLASES; PLANT PROTEINS; PLANTS; SEQUENCE HOMOLOGY, NUCLEIC ACID; TREES;

EID: 0024066667     PISSN: 01773593     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/bchm3.1988.369.2.741     Document Type: Article

References (51)

1. Coodenough, P.W. & Owen, J. (1987)Phytochemistry 26, 75–79.
2. Baines, B.S. & Brocklehurst, K. (1982) J. Prot. Chem. 1, 119–139.
3. Kaarsholm, N.C. & Schack, P. (1983),4cto Chem. Seand. B37, 607–611.
4. Schack, P. (1967) C.R. Trav. Lab. Carlsberg 36, 67–83.
5. Robinson, G.W. (1975) Biochemistry 14, 3695–3700.
6. Brocklehurst, K. & Salih, E. (1983) Biochem. J. 213, 559–560.
7. Polgar, L. (1984)Biochem. J. 221, 555–556.
8. Buttle, D.J. & Barrett, A.J. (1984) Biochem. J. 223, 81–88.
9. Brocklehurst, K. & Salih, E. (1985) Biochem. J. 228, 525–527.
10. Dubois, T., Jacquet, A., Schnek, A.G. & Looze, Y. (1988) Biol. Chem. Hoppe-Seyler 369, 733–740, preceding paper.
11. Lynn, K. R. (1979) Biochim. Biophys. Acta 569, 193–201.
12. Brocklehurst, K., Carey, P.R., Lee, H.H., Salih, E. & Storer, A.C. (1984) Biochem. J. 223, 649–657.
13. Lynn, K.R. & Yaguchi, M. (1979)Biochim. Biophys. Acta 581, 363–364.
14. Schack, P. & Kaarsholm, N.C. (1984) Biochem. J. 219, 727–733.
15. Zucker, S., Buttle, D.J., Nickiin, M.J.H. & Barrett, A. J. (1985) Biochim. Biophys. Acta 828, 196–204.
16. Hirs, C.H.W., Moore, S. & Stein, W.H. (1956) J. Biol. Chem. 219, 623–642.
17. Mancheva, I., Kleinschmidt, T., Aleksiev, B. & Braunitzer, G. (1984) Hoppe-Seyler's Z. Physiol. Chem. 365, 885–894.
18. Kratzin, H., Yang, C., Krusche, J.U. & Hilschmann, N. (1980) Hoppe-Seyler's Z. Physiol. Chem. 361, 1591–1598.
19. Braunitzer, G., Schrank, B., Ruhfus, A., Petersen, S. & Petersen, U. (1971) Hoppe-Seyler's Z. Physiol. Chem. 352, 1730–1732.
20. Edman, P. & Begg, G. (1967) Eur. J. Biochem. 1, 80–91.
21. Hewick, R.M., Hunkapiller, M.W., Hood, L.E. & Dreyer, W. J. (1981) J. Biol. Chem. 256, 7990–7997.
22. Begg, G., Rücknagel, P., Godovac-Zimmermann, J., Braunitzer, G. & Schuster, W. (1986) Biol. Chem. Hoppe-Seyler 367, 81–82.
23. Zimmermann, C.L. & Pisano, J.J. (1977) Methods Enzymol. 47, 45-51.
24. Lottspeich, F. (1980) Hoppe-Seyler's Z. Physiol. Chem. 361, 1829–1834.
25. Akaboris, S., Ohno, K. & Narita, K. (1952) Bull. Chem. Soc. Jpn. 25, 214–218.
26. Kamphuis, I.G., Drenth, J. & Baker, E.N. (1985) J. Mol. Biol. 182, 317–329.
27. Königsberg, W.H. & Steinman, H.M. (1977) in The Proteins (Neurath, H. & Hill, R. L., eds.), 3rd ed., vol. 3, pp. 137-140, Academic Press, New York.
28. Schrohenloher, R. & Bennett, J.C. (1986) in Practical Protein Chemistry -A Handbook (Darbre, A., ed.), pp. 149-164, Wiley-Interscience.
29. Mitchel, E.J., Chaiken, I.M. & Smith, E.L. (1970) J. Biol. Chem. 245, 3485–3492.
30. Carne, A. & Moore, C.H. (1978) Biochem. J. 173, 73–83.
31. Rogers, J.C., Dean, D. & Heck, G.R. (1985)Proc. Natl. Acad. Sci. U.S.A. 82, 6512–6516.
32. Wilhams, J.G., North, M.J. & Mahbubani, H. (1985) EMBOJ. 4, 999–1006.
33. Pears, C.J., Mahbubani, H.M. & Wilhams, J.G. (1985) Nucleic Acids Res. 13, 8853–8866.
34. Tai, J. Y., Kortt, A.A., Liu, T.-Y. & Elliott, S.D. (1976) J. Biol. Chem. 251, 1955–1959.
35. Argos, P., Kamer, G., Nickiin, M.J.H. & Wimmer, E. (1984) Nucleic Acids Res. 12, 7251–7267.
36. Ohno, S., Emori, Y., Imajoh, S., Kawasaki, H., Kisaragi, M. & Suzuki, K. (1984) Nature (London) 312, 566–570.
37. Barrett, A.J. (1986) in Proteinase Inhibitors (Barrett, A.J. & Salvesen, G., eds.), pp. 3–22, Elsevier, Amsterdam.
38. Takio, K., Towatari, T., Katunuma, N., Teller, D.C. & Titani, K. (1983) Proc. Natl. Acad. Sci. U.S.A. 80, 3666–3670.
39. Ritonja, A., Popovic, T., Turk, V., Wiedenmann, K. & Machleidt, W. (1985) FEBS Lett. 181, 169–172.
40. Kamphuis, I.G., Kalk, K.H., Swarte, M.B.A. & Drenth, J. (1984) J. Mol. Biol. 179, 233–257.
41. Baker, E.N. (1980) J. Mol. Biol. 141, 441–484.
42. Cohen, L.W., Coghlan, V.M. & Dihel, L.C. (1986) Gene 48, 219–227.
43. Light, A., Frater, R., Kimmel, J. R. & Smith, E. L. (1964)Proc. Nat. Acad. Sci. U.S.A. 52, 1276–1283.
44. Ramakrishnan, C. & Ramachandran, G.N. (1965) Biophys. J. 5, 909–933.
45. Drenth, J., Jansonius, J.N., Koekoek, R. & Wolthers, B. (1971) Adv. Protein Chem. 25, 79–115.
46. Brocklehurst, K., Baines, B. S. & Kierstan, M. P. J. (1981) Topics in Enzyme and Fermentation Biotechnology 5, 262–335.
47. Berger, A. & Schechter, I. (1970) Phil. Trans. Roy. Soc. Lond. B257, 249–264.
48. Drenth, J., Kalk, K.H. & Swen, H.M. (1976)Biochemistry 15, 3731–3738.
49. Lowe, G. & Whitworth, A. S. (1974) Biochem. J. 141, 503–515.
50. Baker, E.N., Boland, M.J., Calder, P.C. & Hardman, M.J. (1980) Biochim. Biophys. Acta 616, 30–34.
51. North, M.J. (1986) Biochem. J. 238, 623–624.