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Volumn 31, Issue 2, 1996, Pages 173-178

Effect of lyoprotectants on ascorbate oxidase activity after freeze-drying and storage

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EID: 0029174702     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/0032-9592(95)00045-3     Document Type: Article
Times cited : (8)

References (27)
  • 1
    • 0001810664 scopus 로고
    • Springer, Heidelberg
    • Fee, J. A., In Structure and Bonding, Vol. 23. Springer, Heidelberg, 1975, pp. 2-60.
    • (1975) Structure and Bonding , vol.23 , pp. 2-60
    • Fee, J.A.1
  • 2
    • 0017773782 scopus 로고
    • Evidence about the catecholoxidase activity of the enzyme ascorbate oxidase extracted from Cucurbita pepo medullosa
    • Marchesini, A., Cappelletti, P., Canonica, L., Danieli, B. & Tollari, S., Evidence about the catecholoxidase activity of the enzyme ascorbate oxidase extracted from Cucurbita pepo medullosa. Biochim. Biophys. Acta, 44 (1977) 290-300.
    • (1977) Biochim. Biophys. Acta , vol.44 , pp. 290-300
    • Marchesini, A.1    Cappelletti, P.2    Canonica, L.3    Danieli, B.4    Tollari, S.5
  • 4
    • 0000135375 scopus 로고
    • Expression of ascorbic acid oxidase in zucchini squash (Cucurbita pepo L.)
    • Lin, L. S. & Varner, J. E., Expression of ascorbic acid oxidase in zucchini squash (Cucurbita pepo L.). Plant Physiol. 96 (1991) 159-65.
    • (1991) Plant Physiol. , vol.96 , pp. 159-165
    • Lin, L.S.1    Varner, J.E.2
  • 6
    • 0000180083 scopus 로고
    • Primary structure of the xylose-containing N-linked carbohydrate moiety from ascorbic acid oxidase of Cucurbita pepo medullosa
    • D'Andrea, G., Bouwstra, J. B., Kamerling, J. P. & Vliegenthart, J. F. G., Primary structure of the xylose-containing N-linked carbohydrate moiety from ascorbic acid oxidase of Cucurbita pepo medullosa. Glycoconj. J., 5 (1988) 151-7.
    • (1988) Glycoconj. J. , vol.5 , pp. 151-157
    • D'Andrea, G.1    Bouwstra, J.B.2    Kamerling, J.P.3    Vliegenthart, J.F.G.4
  • 7
    • 0022396839 scopus 로고
    • Determination of ascorbic acid with immobilized green zucchini ascorbate oxidase
    • Stevanato, R., Avigliano, L., Finazzi-Agrò, A. & Rigo, A., Determination of ascorbic acid with immobilized green zucchini ascorbate oxidase. Anal. Biochem., 149 (1985) 537-42.
    • (1985) Anal. Biochem. , vol.149 , pp. 537-542
    • Stevanato, R.1    Avigliano, L.2    Finazzi-Agrò, A.3    Rigo, A.4
  • 8
    • 0025116269 scopus 로고
    • Determination of L-ascorbic acid in fruit and vegetable juices by flow injection with immobilized ascorbate oxidase
    • Greenway, G. M. & Ongomo, P., Determination of L-ascorbic acid in fruit and vegetable juices by flow injection with immobilized ascorbate oxidase. Analyst, 115 (1990) 1297-9.
    • (1990) Analyst , vol.115 , pp. 1297-1299
    • Greenway, G.M.1    Ongomo, P.2
  • 9
    • 0021981346 scopus 로고
    • Measurement of urinary oxalate in the presence of ascorbic acid
    • Crawford, G. A., Mahoney, J. F. & Györy, A. Z., Measurement of urinary oxalate in the presence of ascorbic acid. Clin. Chim. Acta, 147 (1985) 51-7.
    • (1985) Clin. Chim. Acta , vol.147 , pp. 51-57
    • Crawford, G.A.1    Mahoney, J.F.2    Györy, A.Z.3
  • 10
    • 0021645811 scopus 로고
    • A new enzymatic determination of serum creatine
    • Suzuky, M. & Yoshida, M., A new enzymatic determination of serum creatine. Clin. Chim. Acta, 140 (1984) 289-94.
    • (1984) Clin. Chim. Acta , vol.140 , pp. 289-294
    • Suzuky, M.1    Yoshida, M.2
  • 12
    • 0019888281 scopus 로고
    • The stabilization of proteins by sucrose
    • Lee, J. C. & Timasheff, S. N., The stabilization of proteins by sucrose. J. Biol. Chem., 256 (1981) 7193-201.
    • (1981) J. Biol. Chem. , vol.256 , pp. 7193-7201
    • Lee, J.C.1    Timasheff, S.N.2
  • 13
    • 0000586259 scopus 로고
    • ed. G. E. W. Wolstenholme & M. O'Conner. J. & A. Churchill, London
    • Brands, J. F., Fu, J. & Nordin, J. H., In The Frozen Cell, ed. G. E. W. Wolstenholme & M. O'Conner. J. & A. Churchill, London, 1970, pp. 189-212.
    • (1970) The Frozen Cell , pp. 189-212
    • Brands, J.F.1    Fu, J.2    Nordin, J.H.3
  • 14
    • 0020449008 scopus 로고
    • A new type of enzyme electrode: The ascorbic acid eliminator electrode
    • Nagy, G., Rice, M. E. & Adams, R. N., A new type of enzyme electrode: the ascorbic acid eliminator electrode. Life Sci., 31 (1982) 2611-6.
    • (1982) Life Sci. , vol.31 , pp. 2611-2616
    • Nagy, G.1    Rice, M.E.2    Adams, R.N.3
  • 15
    • 0000327453 scopus 로고
    • Determination method for L-ascorbic acid in foods with immobilized ascorbate oxidase
    • Esaka, M., Suzuki, K. & Kubota, K., Determination method for L-ascorbic acid in foods with immobilized ascorbate oxidase. Agric. Biol. Chem., 49 (1985) 2955-60.
    • (1985) Agric. Biol. Chem. , vol.49 , pp. 2955-2960
    • Esaka, M.1    Suzuki, K.2    Kubota, K.3
  • 16
    • 0040824451 scopus 로고
    • Spectrophotometric determination based on difference spectra of L-ascorbic acid in plants and animal foods
    • Tono, T. & Fujita, S., Spectrophotometric determination based on difference spectra of L-ascorbic acid in plants and animal foods. Agric. Biol. Chem., 46 (1982) 2953-9.
    • (1982) Agric. Biol. Chem. , vol.46 , pp. 2953-2959
    • Tono, T.1    Fujita, S.2
  • 18
    • 0013661505 scopus 로고
    • Studies on the effect of the incubation conditions, various detergents and protein concentration on the enzymatic activity of N-glycosidase F (glycopeptidase F) and endoglycosidase F
    • Haselbeck, A. & Hösel, W., Studies on the effect of the incubation conditions, various detergents and protein concentration on the enzymatic activity of N-glycosidase F (glycopeptidase F) and endoglycosidase F. Topics Biochem., 8 (1988) 1-4.
    • (1988) Topics Biochem. , vol.8 , pp. 1-4
    • Haselbeck, A.1    Hösel, W.2
  • 19
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72 (1976) 248-54.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 20
    • 0021101963 scopus 로고
    • The effect of freeze-drying on the quaternary structure of L-asparaginase from Erwinia carotovora
    • Hellman, K., Miller, D. S. & Cammack, K. A., The effect of freeze-drying on the quaternary structure of L-asparaginase from Erwinia carotovora. Biochim. Biophys. Acta, 749 (1983) 133-42.
    • (1983) Biochim. Biophys. Acta , vol.749 , pp. 133-142
    • Hellman, K.1    Miller, D.S.2    Cammack, K.A.3
  • 21
    • 0023659990 scopus 로고
    • Stabilization of phosphofructokinase with sugars during freeze-drying: Characterization of enhanced protection in the presence of divalent cations
    • Carpenter, J. F., Crowe, L. M. & Crowe, J. H., Stabilization of phosphofructokinase with sugars during freeze-drying: characterization of enhanced protection in the presence of divalent cations. Biochim. Biophys. Acta, 923 (1987) 109-15.
    • (1987) Biochim. Biophys. Acta , vol.923 , pp. 109-115
    • Carpenter, J.F.1    Crowe, L.M.2    Crowe, J.H.3
  • 22
    • 0002881849 scopus 로고
    • Freeze-drying of proteins. Part I: Process design
    • Pikal, M. J., Freeze-drying of proteins. Part I: Process design. Pharm. Technol. Int., 3 (1) (1991) 37-43.
    • (1991) Pharm. Technol. Int. , vol.3 , Issue.1 , pp. 37-43
    • Pikal, M.J.1
  • 23
    • 0002881849 scopus 로고
    • Freeze-drying of proteins. Part II: Formulation selection
    • Pikal, M. J., Freeze-drying of proteins. Part II: Formulation selection. Pharm. Technol. Int., 3 (2) (1991) 40-3.
    • (1991) Pharm. Technol. Int. , vol.3 , Issue.2 , pp. 40-43
    • Pikal, M.J.1
  • 24
    • 0027519943 scopus 로고
    • Protein glycosylation. Structural and functional aspects
    • Lis, H. & Sharon, N., Protein glycosylation. Structural and functional aspects. Eur. J. Biol., 218 (1993) 1-27.
    • (1993) Eur. J. Biol. , vol.218 , pp. 1-27
    • Lis, H.1    Sharon, N.2
  • 25
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein in enzymatically active form
    • Schägger, H. & von Jagow, G., Blue native electrophoresis for isolation of membrane protein in enzymatically active form. Anal. Biochem., 199 (1991) 223-31.
    • (1991) Anal. Biochem. , vol.199 , pp. 223-231
    • Schägger, H.1    Von Jagow, G.2
  • 26
    • 0028214450 scopus 로고
    • Analysis of molecular masses and oligomeric state of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis
    • Schägger, H., Cramer, W. A. & von Jagow, G., Analysis of molecular masses and oligomeric state of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis. Anal. Biochem., 217 (1994) 220-30.
    • (1994) Anal. Biochem. , vol.217 , pp. 220-230
    • Schägger, H.1    Cramer, W.A.2    Von Jagow, G.3
  • 27
    • 0027909093 scopus 로고
    • Dramatic enhancement of enzymatic activity in organic solvents by lyoprotectants
    • Dabulis, K. & Klibanov, A. M., Dramatic enhancement of enzymatic activity in organic solvents by lyoprotectants. Biotechnol. Bioeng., 41 (1993) 566-71.
    • (1993) Biotechnol. Bioeng. , vol.41 , pp. 566-571
    • Dabulis, K.1    Klibanov, A.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.