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Volumn 45, Issue 4, 2004, Pages 275-283

Purification and characterization of isoforms of β-N- acetylhexosaminidase from mungbean seedlings

Author keywords

N acetylhexosaminidase; Enzyme purification; Germination; Oligomeric structure; Vigna radiata

Indexed keywords

PHASEOLUS (ANGIOSPERM); VIGNA; VIGNA RADIATA; VIGNA RADIATA VAR. RADIATA;

EID: 9244251608     PISSN: 00068063     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (7)

References (32)
  • 1
    • 0014408293 scopus 로고
    • Glycosidases of Phaseolus vulgaris. II. Isolation and general properties
    • Agrawal, K.M.L. and O.P. Bahl. 1968. Glycosidases of Phaseolus vulgaris. II. Isolation and general properties. J. Biol. Chem. 243: 103-111.
    • (1968) J. Biol. Chem. , vol.243 , pp. 103-111
    • Agrawal, K.M.L.1    Bahl, O.P.2
  • 2
    • 0001684417 scopus 로고
    • α-Galactosidase, β-glucosidase, β-N- acetylglucosaminidase, and α-mannosidase from pinto beans (Phaseolus vulgaris)
    • Agrawal, K.M.L. and O.P. Bahl. 1972. α-Galactosidase, β-glucosidase, β-N-acetylglucosaminidase, and α-mannosidase from pinto beans (Phaseolus vulgaris). Methods Enzymol. 28: 720-728.
    • (1972) Methods Enzymol. , vol.28 , pp. 720-728
    • Agrawal, K.M.L.1    Bahl, O.P.2
  • 3
    • 0014408278 scopus 로고
    • Glycosidases of Phaseolus vulgaris 1. Isolation and characterization of β-N-acetylglucosaminidase
    • Bahl, O.P. and K.M.L. Agrawal. 1968. Glycosidases of Phaseolus vulgaris 1. Isolation and characterization of β-N-acetylglucosaminidase. J. Biol. Chem. 243: 98-102.
    • (1968) J. Biol. Chem. , vol.243 , pp. 98-102
    • Bahl, O.P.1    Agrawal, K.M.L.2
  • 5
    • 0017811848 scopus 로고
    • Properties of four molecular forms of N-acetyl-β-D-hexosaminidase isolated from germinating seeds of fenugreek (Trigonella foenum graecum)
    • Bouquelet, S. and G. Spik. 1978. Properties of four molecular forms of N-acetyl-β-D-hexosaminidase isolated from germinating seeds of fenugreek (Trigonella foenum graecum). Eur. J. Biochem. 84:551-559.
    • (1978) Eur. J. Biochem. , vol.84 , pp. 551-559
    • Bouquelet, S.1    Spik, G.2
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principles of protein-dye binding
    • Bradford, M.M. 1976. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principles of protein-dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0342972186 scopus 로고
    • Comparison of some molecular, enzymatic and antifungal properties of chitinases from thom-apple, tobacco and wheat
    • Broekaert, W.F., J.V. Parijs, A.K. Allen, and W.J. Peumans. 1988. Comparison of some molecular, enzymatic and antifungal properties of chitinases from thom-apple, tobacco and wheat. Physiol. Mol. Plant Phathol. 33: 319-331.
    • (1988) Physiol. Mol. Plant Phathol. , vol.33 , pp. 319-331
    • Broekaert, W.F.1    Parijs, J.V.2    Allen, A.K.3    Peumans, W.J.4
  • 8
    • 0031821133 scopus 로고    scopus 로고
    • Purification and properties of β-N-acetylhexosaminidase from cabbage
    • Chang, C.T., F.P. Young, M.H. Chang, and H.Y. Sung. 1998. Purification and properties of β-N-acetylhexosaminidase from cabbage. Biochem. Mol. Biol. Int. 45: 371-380.
    • (1998) Biochem. Mol. Biol. Int. , vol.45 , pp. 371-380
    • Chang, C.T.1    Young, F.P.2    Chang, M.H.3    Sung, H.Y.4
  • 9
    • 0028038899 scopus 로고
    • N-Acetyl-β-D-glucosaminidase from "golden delicious" apples
    • Choi, S.Y and K.C. Gross. 1994. N-Acetyl-β-D-glucosaminidase from "golden delicious" apples. Phytochemistry 36: 1-6.
    • (1994) Phytochemistry , vol.36 , pp. 1-6
    • Choi, S.Y.1    Gross, K.C.2
  • 11
    • 0023074051 scopus 로고
    • Glycolipid and glycoprotein degradation
    • A. Meister (ed.), John Wiley & Sons, New York, Chichester, Brisbane, Toronto, Singapore
    • Conzelmann, E. and K. Sandhoff. 1987. Glycolipid and glycoprotein degradation. In A. Meister (ed.), Adv. Enzymol. vol. 60. John Wiley & Sons, New York, Chichester, Brisbane, Toronto, Singapore, pp. 89-216.
    • (1987) Adv. Enzymol. , vol.60 , pp. 89-216
    • Conzelmann, E.1    Sandhoff, K.2
  • 12
    • 0001355337 scopus 로고
    • Occurrence of glycoprotein glycosidases in mature seeds of mungbean (Vigna radiata)
    • Dey, P.M. 1984. Occurrence of glycoprotein glycosidases in mature seeds of mungbean (Vigna radiata). Phytochemistry 23: 257-260.
    • (1984) Phytochemistry , vol.23 , pp. 257-260
    • Dey, P.M.1
  • 13
    • 0021306831 scopus 로고
    • Biochemistry of the multiforms of glycosidases in plants
    • A. Meister (ed.), John Wiley and sons, New York, Chichester, Brisbane, Toronto, Singapore
    • Dey, P.M. and E.D. Campillo. 1984. Biochemistry of the multiforms of glycosidases in plants. In A. Meister (ed.), Adv. Enzymol. Vol. 54. John Wiley and sons, New York, Chichester, Brisbane, Toronto, Singapore, pp. 141-249.
    • (1984) Adv. Enzymol. , vol.54 , pp. 141-249
    • Dey, P.M.1    Campillo, E.D.2
  • 15
    • 0010582302 scopus 로고
    • β-N-Acetylhexosaminidase from soybean
    • Gers-Barlag, H., I. Bartz, and H. Rüdiger. 1988. β-N-Acetylhexosaminidase from soybean. Phytochemistry 27: 3739-3741.
    • (1988) Phytochemistry , vol.27 , pp. 3739-3741
    • Gers-Barlag, H.1    Bartz, I.2    Rüdiger, H.3
  • 16
    • 0002087092 scopus 로고
    • Purification and properties of N-acetyl-β-D-glucosaminidase from Hevea brasiliensis latex
    • Giordani, R., S. Benyahia, M. Teissere, and G. Noat. 1992. Purification and properties of N-acetyl-β-D-glucosaminidase from Hevea brasiliensis latex. Plant Sci. 84: 25-34.
    • (1992) Plant Sci. , vol.84 , pp. 25-34
    • Giordani, R.1    Benyahia, S.2    Teissere, M.3    Noat, G.4
  • 18
    • 0142095633 scopus 로고
    • Characterization and partial purification of three glycosidases from castor bean endosperm
    • Harley, S.M. and H. Beevers. 1985. Characterization and partial purification of three glycosidases from castor bean endosperm. Phytochemistry 24: 1459-1464.
    • (1985) Phytochemistry , vol.24 , pp. 1459-1464
    • Harley, S.M.1    Beevers, H.2
  • 19
    • 4243428956 scopus 로고
    • Isozymes of β-N-acetylhexosaminidase from pea seeds (Pisum sativum L.)
    • Harley, S.M. and L. Beevers. 1987. Isozymes of β-N- acetylhexosaminidase from pea seeds (Pisum sativum L.). Plant Physiol. 85: 1118-1122.
    • (1987) Plant Physiol. , vol.85 , pp. 1118-1122
    • Harley, S.M.1    Beevers, L.2
  • 20
    • 0030039108 scopus 로고    scopus 로고
    • Measurement in situ of chitinase and β-N-acetylglucosaminidae activities in germinating-seeds of Pinus sylvestris and Eucalyptus pilularis
    • Hodge, A., I.J. Alexander, and G.W. Gooday. 1996. Measurement in situ of chitinase and β-N-acetylglucosaminidae activities in germinating-seeds of Pinus sylvestris and Eucalyptus pilularis. Plant Physiol. Biochem. 34: 301-306.
    • (1996) Plant Physiol. Biochem. , vol.34 , pp. 301-306
    • Hodge, A.1    Alexander, I.J.2    Gooday, G.W.3
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structure proteins during the assembly of the head of the bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structure 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
  • 22
    • 0035371613 scopus 로고    scopus 로고
    • Purification and characterization of isoforms of β-galactosidases in mungbean seedlings
    • Li, S.C., J.W. Han, K.C. Chen, and C.S. Chen. 2001. Purification and characterization of isoforms of β-galactosidases in mungbean seedlings. Phytochemistry 57: 349-359.
    • (2001) Phytochemistry , vol.57 , pp. 349-359
    • Li, S.C.1    Han, J.W.2    Chen, K.C.3    Chen, C.S.4
  • 23
    • 0014940534 scopus 로고
    • Studies on the glycosidases of jack bean meal III. Crystallization and properties of β-N-acetylhexosaminidase
    • Li, S.C. and Y.T. Li. 1970. Studies on the glycosidases of jack bean meal III. crystallization and properties of β-N-acetylhexosaminidase. J. Biol. Chem. 245: 5153-5160.
    • (1970) J. Biol. Chem. , vol.245 , pp. 5153-5160
    • Li, S.C.1    Li, Y.T.2
  • 25
    • 0344566247 scopus 로고
    • Purification and properties of a β-N-acetylaminoglucohydrolase from malted barley
    • Mitchell, E.D., C.W. Houston, and S.B. Latimer. 1976. Purification and properties of a β-N-acetylaminoglucohydrolase from malted barley. Phytochemistry 15: 1869-1871.
    • (1976) Phytochemistry , vol.15 , pp. 1869-1871
    • Mitchell, E.D.1    Houston, C.W.2    Latimer, S.B.3
  • 26
    • 0010617350 scopus 로고
    • Glycosidases from cotyledons of Pisum sativum L.
    • Neely, R.S. and L. Beevers. 1980. Glycosidases from cotyledons of Pisum sativum L. J. Exp. Bot. 31: 299-312.
    • (1980) J. Exp. Bot. , vol.31 , pp. 299-312
    • Neely, R.S.1    Beevers, L.2
  • 27
    • 0344997252 scopus 로고
    • The lysosome-concept in plants II. Location of acid hydrolases in maize root tips
    • Parish, R.W. 1975. The lysosome-concept in plants II. Location of acid hydrolases in maize root tips. Planta 123: 15-31.
    • (1975) Planta , vol.123 , pp. 15-31
    • Parish, R.W.1
  • 28
    • 0010635255 scopus 로고
    • Partial purification and characterization of a β-N- acetylhexosaminidase from black cherry (Prunus serotina ehrh) seeds
    • Poulton, J.E., M.A. Thomas, K.K. Ottwell, and S.J. MeCormick. 1985. Partial purification and characterization of a β-N-acetylhexosaminidase from black cherry (Prunus serotina ehrh) seeds. Plant Sci. 42: 107-114.
    • (1985) Plant Sci. , vol.42 , pp. 107-114
    • Poulton, J.E.1    Thomas, M.A.2    Ottwell, K.K.3    Mecormick, S.J.4
  • 29
    • 0023901367 scopus 로고
    • Cloning and expression of a Streptomyces plicatus chitinase (chitinase-63) in Escherichia coli
    • Robbins, P.W., C. Albright, and B. Benfield. 1988. Cloning and expression of a Streptomyces plicatus chitinase (chitinase-63) in Escherichia coli. J. Biol. Chem. 263: 443-447.
    • (1988) J. Biol. Chem. , vol.263 , pp. 443-447
    • Robbins, P.W.1    Albright, C.2    Benfield, B.3
  • 30
    • 0001519173 scopus 로고
    • Plant chitinases are potent inhibitors of fungal growth
    • Schlumbaum, A., F. Mauch, U. Vogeli, and T. Boller. 1986. Plant chitinases are potent inhibitors of fungal growth. Nature 324: 365-367.
    • (1986) Nature , vol.324 , pp. 365-367
    • Schlumbaum, A.1    Mauch, F.2    Vogeli, U.3    Boller, T.4
  • 31
    • 0021274996 scopus 로고
    • Transient N-acetylglucosamine in the biosynthesis of phytohemagglutinin: Attachment in the Golgi apparatus and removal in protein bodies
    • Vitale, A. and M. J. Chrispeels. 1984. Transient N-acetylglucosamine in the biosynthesis of phytohemagglutinin: attachment in the Golgi apparatus and removal in protein bodies. J. Cell Biol. 99: 133-140.
    • (1984) J. Cell Biol. , vol.99 , pp. 133-140
    • Vitale, A.1    Chrispeels, M.J.2
  • 32
    • 0010614149 scopus 로고
    • Increase in β-N-acetylglucosaminidase activity during germination of cotton seeds
    • Yi, C.K. 1981. Increase in β-N-acetylglucosaminidase activity during germination of cotton seeds. Plant Physiol. 67: 68-73.
    • (1981) Plant Physiol. , vol.67 , pp. 68-73
    • Yi, C.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.