The primary structure and characterization of carbohydrate chains of the extracellular glycoprotein proteinase inhibitor from latex of Carica papaya

European Journal of Biochemistry

Volumn 241, Issue 1, 1996, Pages 77-82

  Odani, Shoji ^a   Yokokawa, Yayoi ^a   Takeda, Hiroshi ^a   Abe, Sachiko ^a   Odani, Sumiko ^a  

^a NIIGATA UNIVERSITY   (Japan)

Author keywords

Chymotrypsin inhibitor; Hydrophilic peptide; Mass spectrometry; Methylation; Soybean trypsin inhibitor

Indexed keywords

CHYMOTRYPSIN A; MIRACULIN; PROTEINASE INHIBITOR; SWEETENING AGENT; TRYPSIN; UNCLASSIFIED DRUG;

AMINO ACID COMPOSITION; ARTICLE; BINDING SITE; CARBOHYDRATE ANALYSIS; DISULFIDE BOND; DRUG ISOLATION; DRUG PURIFICATION; ENZYME INHIBITION; IN VITRO STUDY; MASS SPECTROMETRY; PHYTOCHEMISTRY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FAMILY; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; TECHNIQUE;

BOVINAE; CARICA PAPAYA; GLYCINE MAX;

EID: 0029843544     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0077t.x     Document Type: Article

References (32)

1. Carrell, R. W. & Boswell, D. R. (1986) Serpins: the superfamily of plasma serine proteinase inhibitors, in Proteinase inhibitors (Barrett, A. J. & Salvesen, G., eds) pp. 403-420, Elsevier, Amsterdam.
2. Richardson, M. (1977) The proteinase inhibitors of plants and microorganisms, Phytochemistry (Oxf.) 16, 159-169.
3. Ryan, C. A. (1973) Proteolytic enzymes and their inhibitors in plants, Annu. Rev. Plant. Physiol. 24, 173-196.
4. Bishop, P. D., Makus, D. J., Pearce, G. & Ryan, C. A. (1981) Proteinase inhibitor-inducing factor activity in tomato leaves resides in oligosaccharides enzymically released from cell walls, Proc. Natl Acad. Sci. USA, 78, 3356-3540.
5. Graham, J. S., Pearce, G., Meryweather, J., Titani, K., Ericsson, L. & Ryan, C. A. (1985) Wound-induced proteinase inhibitors from tomato leaves. I. The cDNA-deduced primary structure of pre-inhibitor I and its post-translational processing. J. Biol. Chem. 260, 6555-6560.
6. Reddy, M. N., Keim, P. S., Heinrikson, R. L. & Kezdy, F. J. (1975) Primary structural analysis of sulfhydryl protease inhibitors from pineapple stem, J. Biol. Chem. 250, 1741-1750.
7. Odani, S., Koide, T. & Ono, T. (1986) Wheat germ trypsin inhibitors. Isolation and structural characterization of single-headed and double-headed inhibitors of the Bowman-Birk type, J. Biochem. (Tokyo) 100, 975-983.
8. Hirs, C. H. W.(1967) Reduction and S-carboxymethylation of proteins, Methods Enzymol. 11, 199-203.
9. Ui, N. (1979) Rapid estimation of the molecular mass of protein polypeptide chains using high-pressure liquid chromatography in 6 M guanidine hydrochloride. Anal. Biochem. 97, 65-71.
10. Narita, K., Matsuo, H. & Nakajima, T. (1975) End group determination, in Protein Sequence Determination (Needleman, S. B., ed.) pp. 30-103, Springer-Verlag, Berlin.
11. Matsubara, H. & Sasaki, R. M. (1965) High recovery of tryptophan from acid hydrolysates of proteins, Biochem. Biophys. Res. Commun. 35, 175-181.
12. Hase, S., Ibuki, T. & Ikenaka, T. (1984) Reexamination of the pyridylamination used for fluorescence labeling of oligosaccharides and its application to glycopeptides, J. Biochem. (Tokyo) 95, 197-203.
13. Laskowski, M. Jr & Kato, I. (1980) Protein inhibitors of proteinases, Annu. Rev. Biochem. 49, 593-626.
14. Tarentino, A. L., Gomez, C. M. & Plummers, T. H. Jr (1985) Degly-cosylation of asparagine-linked glycans by peptide N-glycosidase F, Biochemistry 24, 4655-4671.
15. Hase, S., Koyama, S., Daiyasu, H., Takammoto, H., Hara, S., Kobayashi, Y., Kyogoku, Y. & Ikenaka, T. (1986) Structure of a sugar chain of a protease inhibitor isolated from Barbados pride (Caesalpinia pulcherrinma Sw.) seeds, J. Biochem. (Tokyo) 100, 1-12.
16. Tezuka, K., Hayashi, M., Ishihara, H., Akazawa, T. & Takahashi, N. (1992) Studies on synthetic pathway of xylose-containing N-linked oligosaccharides deduced form substrate specificities of the processing enzymes in sycamore cells (Acer pseudoplatanus L.) Eur. J. Biochem. 203, 401-413.
17. Hayashi, M., Tsuru, A., Mitsui, T., Takahashi, N., Hanzawa, H., Arata, Y. & Akazawa, T. (1990) Structure and biosynthesis of the xylose-containing carbohydrate moiety of rice α-amylase, Eur. J. Biochem. 191, 287-295.
18. Driouich, A., Loiec, F. & Staehelin, A. (1993) The plant Golgi apparatus: a factory for complex polysaccharides and glycoproteins, Trends Bichem. Sci. 19, 210-214.
19. Faye, L., Johnson, K. D., Sturm, A. & Chrispeels, M. J. (1989) Structure, biosynthesis, and functions of asparagine-linked glycans on plant glycoproteins, Physiol. Plant. 75, 309-314.
20. Koide, T. & Ikenaka, T. (1973) Studies on soybean trypsin inhibitors 3. Amino acid sequence of the carboxyl-terminal region and the complete amino acid sequence of soybean lrypsin inhibitor (Kunitz), Eur. J. Biochem. 32, 417-431.
21. Hejgaard, H., Svendsen, I. & Mundy, J. (1983) Barley α-amylase/ subtilisin inhibitor. II. N-terminal amino acid sequence and homology with inhibitors of the soybean trypsin inhibitor (Kunitz) family, Carlsberg Res. Commun. 48, 91-94.
22. Theerasilp, S., Hitotsuya, H., Nakajo, S., Nakaya, K., Nakamura, Y. & Kurihara, Y. (1988) Complete amino acid sequence and structure characterization of the taste-modifying protein, Miraculin, J. biol. Chem. 264, 6655-6659.
23. Hattori, T., Yoshida, N. & Nakamura, K. (1989) Structural relationship among the members of a multigene family coding for the sweet potato tuberous root storage protein, Plant Mol. Biol. 13, 563-572.
24. Stiekema, W. J., Heidekamp, F., Dirkse, W. G., van Beckum, J., de Haan, P., ten Bosch, C. & Louwerse, J. D. (1988) Molecular cloning and analysis of four potato tuber mRNAs, Plant Mol. Biol. 11, 255-269.
25. Bradshow, H. D. Jr, Hollick, J. B., Pearson, T. J., Clarke, H. R. G. & Gordon, M. P. (1989) Systemically wound-responsive genes in poplar trees encode proteins similar to sweet potato sporamins and legume Kunitz trypsin inhibitors. Plant Mol. Biol. 14, 51-59.
26. Strukelj, B., Pungercar, J., Mesko, P., Barlic-Maganja, D., Gubensek, F., Kregar, I. & Turk V. (1992) Characterization of aspartic proteinase inhibitors from potato at the gene, cDNA and protein levels, Biol. Chem. Hoppe-Seyler 373, 477-482.
27. Reference deleted.
28. Krizaj, I., Drobnic-Kosorok, M., Brzin, J., Jerala, R. & Turk, V. (1993) The primary structure of inhibitor of cysteine proteinases from potato, FEBS Lett. 333, 15-20.
29. Trumper, S., Follmann, H. & Haberlein, I. (1994) A novel dehydroascorbate reductase from spinach chloroplasts homologous to plant trypsin inhibitor, FEBS Lett. 352, 159-162.
30. Johnstone, E. M., Chancy, M. O., Moore, R. E., Ward, K. E., Norris, F. H. & Little, S. P. (1989) Alzheimer's disease amyloid peptide is encoded by two exons and shows similarity to soybean trypsin inhibitor. Biochem. Biophys. Res. Commun. 163, 1248-1255.
31. Onesti, S., Brick, P. & Blow, D. M. (1991) Crystal structure of a Kunitz-type trypsin inhibitor from Erythrina caffra seeds, J. Mol. Biol. 217, 153-176.
32. Thompson, J. B., Higgins, D. G. & Gibson, T. J. (1994) Clustal W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680.