메뉴 건너뛰기




Volumn 243, Issue 3, 1997, Pages 695-700

The glycosylation of the aspartic proteinases from barley (Hordeum vulgare L.) and cardoon (Cynara cardunculus L.)

Author keywords

Aspartic proteinase; Cynara cardunculus; Glycosylation; Hordeum vulgare

Indexed keywords

ASPARTIC PROTEINASE;

EID: 0031023724     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.t01-1-00695.x     Document Type: Article
Times cited : (46)

References (28)
  • 1
    • 0025033985 scopus 로고
    • Effects of glycosylation on the secretion and enzyme activity of Mucor rennin, an aspartic proteinase of Mucor pusillus, produced by recombinant yeast
    • Aikawa, J., Yamashita, T., Nishiyama, M., Horinouchi, S. & Beppu, T. (1990) Effects of glycosylation on the secretion and enzyme activity of Mucor rennin, an aspartic proteinase of Mucor pusillus, produced by recombinant yeast, J. Biol. Chem. 265, 13955–13959.
    • (1990) J. Biol. Chem. , vol.265 , pp. 13955-13959
    • Aikawa, J.1    Yamashita, T.2    Nishiyama, M.3    Horinouchi, S.4    Beppu, T.5
  • 2
    • 0029101380 scopus 로고
    • Rice aspartic proteinase, oryzasin, expressed during seed ripening and germination, has a gene organization distinct from those of animal and microbial aspartic proteinases
    • Asakura, T., Watanabe, H., Abe, K. & Arai, S. (1995) Rice aspartic proteinase, oryzasin, expressed during seed ripening and germination, has a gene organization distinct from those of animal and microbial aspartic proteinases, Eur. J. Biochem. 232, 77–83.
    • (1995) Eur. J. Biochem. , vol.232 , pp. 77-83
    • Asakura, T.1    Watanabe, H.2    Abe, K.3    Arai, S.4
  • 4
    • 0017277818 scopus 로고
    • Assay of proteins in the presence of interfering materials
    • Bensadoun, A. & Weinstein, D. (1976) Assay of proteins in the presence of interfering materials, Anal. Biochem. 70, 241–250.
    • (1976) Anal. Biochem. , vol.70 , pp. 241-250
    • Bensadoun, A.1    Weinstein, D.2
  • 5
    • 0025784815 scopus 로고
    • The development of Aspergillus niger var. awamori as a host for the expression and secretion of heterologous gene products
    • Berka, R. M., Kodama, K. H., Rey, M. W., Wilson, L. J. & Ward, M. (1991) The development of Aspergillus niger var. awamori as a host for the expression and secretion of heterologous gene products, Biochem. Soc. Trans. 19, 681–685.
    • (1991) Biochem. Soc. Trans. , vol.19 , pp. 681-685
    • Berka, R.M.1    Kodama, K.H.2    Rey, M.W.3    Wilson, L.J.4    Ward, M.5
  • 6
    • 0029164230 scopus 로고
    • Nonselective and efficient fluorescent labeling of glycans using 2‐aminobenzamide and anthranilic acid
    • Bigge, J. C., Patel, T. P., Bruce, J. A., Goulding, P. N., Charles, S. M. & Parekh, R. B. (1995) Nonselective and efficient fluorescent labeling of glycans using 2‐aminobenzamide and anthranilic acid, Anal. Biochem. 230, 229–238.
    • (1995) Anal. Biochem. , vol.230 , pp. 229-238
    • Bigge, J.C.1    Patel, T.P.2    Bruce, J.A.3    Goulding, P.N.4    Charles, S.M.5    Parekh, R.B.6
  • 7
    • 0028387411 scopus 로고
    • Isolation and characterization of a cDNA from flowers of Cynara cardunculus encoding cyprosin (an aspartic proteinase) and its use to study the organ‐specific expression of cyprosin
    • Cordeiro, M. C., Xue, Z., Pietrzak, M., Pais, M. S. & Brodelius, P. E. (1994) Isolation and characterization of a cDNA from flowers of Cynara cardunculus encoding cyprosin (an aspartic proteinase) and its use to study the organ‐specific expression of cyprosin, Plant Mol. Biol. 24, 733–741.
    • (1994) Plant Mol. Biol. , vol.24 , pp. 733-741
    • Cordeiro, M.C.1    Xue, Z.2    Pietrzak, M.3    Pais, M.S.4    Brodelius, P.E.5
  • 8
    • 0025290527 scopus 로고
    • The structure and function of the aspartic proteinases
    • Davies, D. R. (1990) The structure and function of the aspartic proteinases, Annu. Rev. Biophys. Chem. 19, 189–215.
    • (1990) Annu. Rev. Biophys. Chem. , vol.19 , pp. 189-215
    • Davies, D.R.1
  • 9
    • 0019882134 scopus 로고
    • Deglycosylation of glycoproteins by trifluoromethanesulfonic acid
    • Edge, A. S. B., Faltynek, C. R., Hof, L., Reichert, L. E. & Weber, P. (1981) Deglycosylation of glycoproteins by trifluoromethanesulfonic acid, Anal. Biochem. 118, 131–137.
    • (1981) Anal. Biochem. , vol.118 , pp. 131-137
    • Edge, A.S.B.1    Faltynek, C.R.2    Hof, L.3    Reichert, L.E.4    Weber, P.5
  • 10
    • 0022186574 scopus 로고
    • Characterization of N‐linked oligosaccharides by affinoblotting with concanavalin A‐peroxidase and treatment of the blots with glycosidases
    • Faye, L. & Chrispeels, M. J. (1985) Characterization of N‐linked oligosaccharides by affinoblotting with concanavalin A‐peroxidase and treatment of the blots with glycosidases, Anal. Biochem. 149, 218–224.
    • (1985) Anal. Biochem. , vol.149 , pp. 218-224
    • Faye, L.1    Chrispeels, M.J.2
  • 12
    • 0027296753 scopus 로고
    • Biosynthesis and secretion of human interleukin 2 glycoprotein variants from baculovirus‐infected Sf21 cells
    • Grabenhorst, E., Hofer, B., Nimtz, M., Jäger, V. & Conradt, H. S. (1993) Biosynthesis and secretion of human interleukin 2 glycoprotein variants from baculovirus‐infected Sf21 cells, Eur. J. Biochem. 215, 189–197.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 189-197
    • Grabenhorst, E.1    Hofer, B.2    Nimtz, M.3    Jäger, V.4    Conradt, H.S.5
  • 13
    • 0028108664 scopus 로고
    • Comparative modelling of barley‐grain aspartic proteinase: a structural rationale for observed hydrolytic specificity
    • Guruprasad, K., Törmäkangas, K., Kervinen, J. & Blundell, T. L. (1994) Comparative modelling of barley‐grain aspartic proteinase: a structural rationale for observed hydrolytic specificity, FEBS Lett. 352, 131–136.
    • (1994) FEBS Lett. , vol.352 , pp. 131-136
    • Guruprasad, K.1    Törmäkangas, K.2    Kervinen, J.3    Blundell, T.L.4
  • 14
    • 0022744765 scopus 로고
    • Structure of a sugar chain of a protease inhibitor isolated from barbados pride (Caesalpinia pulcherrima sw) seeds
    • Hase, S., Koyama, S., Daiyasu, H., Takemoto, H., Hara, S., Kobayashi, Y., Kyogoku, Y. & Ikenaka, T. (1986) Structure of a sugar chain of a protease inhibitor isolated from barbados pride (Caesalpinia pulcherrima sw) seeds, J. Biochem. (Tokyo) 100, 1–10.
    • (1986) J. Biochem. (Tokyo) , vol.100 , pp. 1-10
    • Hase, S.1    Koyama, S.2    Daiyasu, H.3    Takemoto, H.4    Hara, S.5    Kobayashi, Y.6    Kyogoku, Y.7    Ikenaka, T.8
  • 15
    • 0023907932 scopus 로고
    • Role of N‐linked oligosaccharides attached to human renin expressed in COS cells
    • Hori, H., Yoshino, T., Ishizuka, Y., Yamauchi, T. & Murakami, K. (1988) Role of N‐linked oligosaccharides attached to human renin expressed in COS cells, FEBS Lett. 232, 391–394.
    • (1988) FEBS Lett. , vol.232 , pp. 391-394
    • Hori, H.1    Yoshino, T.2    Ishizuka, Y.3    Yamauchi, T.4    Murakami, K.5
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of the bacteriophage T4, Nature 227, 680–685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 33751028137 scopus 로고
    • Specificity and kinetics of the milk‐clotting enzyme from cardoon (Cynara cardunculus L.) towards bovine κ‐casein
    • Macedo, I. Q., Faro, C. J. & Pires, E. (1993) Specificity and kinetics of the milk‐clotting enzyme from cardoon (Cynara cardunculus L.) towards bovine κ‐casein, J. Agric. Food Chem. 41, 1537–1540.
    • (1993) J. Agric. Food Chem. , vol.41 , pp. 1537-1540
    • Macedo, I.Q.1    Faro, C.J.2    Pires, E.3
  • 18
    • 0027414640 scopus 로고
    • Two crystal structures for cathepsin D: the lysosomal targeting signal and active site
    • Metcalf, P. & Fusek, M. (1993) Two crystal structures for cathepsin D: the lysosomal targeting signal and active site, EMBO J. 12, 1293–1302.
    • (1993) EMBO J. , vol.12 , pp. 1293-1302
    • Metcalf, P.1    Fusek, M.2
  • 19
    • 0019273845 scopus 로고
    • Purification and properties of proteinase A from yeast
    • Meussdoerffer, F., Tortora, P. & Holzer, H. (1980) Purification and properties of proteinase A from yeast, J. Biol. Chem. 255, 12087–12093.
    • (1980) J. Biol. Chem. , vol.255 , pp. 12087-12093
    • Meussdoerffer, F.1    Tortora, P.2    Holzer, H.3
  • 20
    • 0000115836 scopus 로고
    • Glycoproteins, in: Carbohydrate analysis
    • Montreuil, J., Bouquelet, S., Debray, H., Fournet, B., Spit, G. & Strecker, G. (1986) Glycoproteins, in Carbohydrate analysis ( Chaplin, M. F. & Kennedy, J. F., eds) pp. 143–204, IRL Press, Oxford.
    • (1986) , pp. 143-204
    • Montreuil, J.1    Bouquelet, S.2    Debray, H.3    Fournet, B.4    Spit, G.5    Strecker, G.6
  • 21
    • 0029000740 scopus 로고
    • Swaposins: circular permutations within genes encoding saposin homologues
    • Ponting, C. P. & Russell, R. B. (1995) Swaposins: circular permutations within genes encoding saposin homologues, Trends Biochem. Sci. 20, 179–180.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 179-180
    • Ponting, C.P.1    Russell, R.B.2
  • 22
    • 0028425479 scopus 로고
    • The aspartic proteinase of barley is a vacuolar enzyme that processes probarley lectin in vitro
    • Runeberg‐Roos, P., Kervinen, J., Kovaleva, V., Raikhel, N. V. & Gal, S. (1994) The aspartic proteinase of barley is a vacuolar enzyme that processes probarley lectin in vitro, Plant Physiol. 105, 321–329.
    • (1994) Plant Physiol. , vol.105 , pp. 321-329
    • Runeberg‐Roos, P.1    Kervinen, J.2    Kovaleva, V.3    Raikhel, N.V.4    Gal, S.5
  • 23
    • 0026321028 scopus 로고
    • Primary structure of a barley‐grain aspartic proteinase
    • Runeberg‐Roos, P., Törmäkangas, K. & Östman, A. (1991) Primary structure of a barley‐grain aspartic proteinase, Eur. J. Biochem. 202, 1021–1027.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 1021-1027
    • Runeberg‐Roos, P.1    Törmäkangas, K.2    Östman, A.3
  • 24
    • 0000296581 scopus 로고
    • Aspartic proteinase from barley grains is related to mammalian lysosomal cathepsin D
    • Sarkkinen, P., Kalkkinen, N., Tilgmann, C., Siuro, J., Kervinen, J. & Mikola, L. (1992) Aspartic proteinase from barley grains is related to mammalian lysosomal cathepsin D, Plant 186, 317–323.
    • (1992) Plant , vol.186 , pp. 317-323
    • Sarkkinen, P.1    Kalkkinen, N.2    Tilgmann, C.3    Siuro, J.4    Kervinen, J.5    Mikola, L.6
  • 25
    • 0020491195 scopus 로고
    • Oligosaccharide accessibility to peptide: N‐glycosidase as promoted by protein‐unfolding reagents
    • Tarentino, A. L. & Plummer, T. H. (1982) Oligosaccharide accessibility to peptide: N‐glycosidase as promoted by protein‐unfolding reagents, J. Biol. Chem. 257, 10776–10780.
    • (1982) J. Biol. Chem. , vol.257 , pp. 10776-10780
    • Tarentino, A.L.1    Plummer, T.H.2
  • 26
    • 0028317608 scopus 로고
    • Tissue‐specific localization of aspartic proteinase in developing and germinating barley grains
    • Tórmäkangas, K., Kervinen, J., Östman, A., Teeri, T. (1994) Tissue‐specific localization of aspartic proteinase in developing and germinating barley grains, Planta 195, 116–125.
    • (1994) Planta , vol.195 , pp. 116-125
    • Tórmäkangas, K.1    Kervinen, J.2    Östman, A.3    Teeri, T.4
  • 27
  • 28
    • 0030060726 scopus 로고    scopus 로고
    • Purification, characterization and partial amino acid sequencing of two new aspartic proteinases from fresh flowers of Cynara cardunculus L.
    • Veríssimo, P., Faro, C., Moir, A. J. G., Lin, Y., Tang, J. & Pires, E. (1996) Purification, characterization and partial amino acid sequencing of two new aspartic proteinases from fresh flowers of Cynara cardunculus L., Eur. J. Biochem. 235, 762–768.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 762-768
    • Veríssimo, P.1    Faro, C.2    Moir, A.J.G.3    Lin, Y.4    Tang, J.5    Pires, E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.