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Volumn 166, Issue 1, 2013, Pages 15-22

Characterization of an α-glucosidase, HdAgl, from the digestive fluid of Haliotis discus hannai

Author keywords

Abalone; Gastropod; GHF31; Haliotis; Glucosidase

Indexed keywords

ALPHA GLUCOSIDASE; AMMONIUM SULFATE; AMYLASE; COMPLEMENTARY DNA; GLUCOPYRANOSIDE; GLUCOSE; MALTOSE; OLIGOSACCHARIDE; POLYMER; STARCH; 4-NITROPHENYL ALPHA-GLUCOSIDE; GLUCOSIDE; MALTOOLIGOSACCHARIDES;

EID: 84879824543     PISSN: 10964959     EISSN: 18791107     Source Type: Journal    
DOI: 10.1016/j.cbpb.2013.06.002     Document Type: Article
Times cited : (7)

References (21)
  • 1
    • 33644510085 scopus 로고    scopus 로고
    • Hydrolyses and transglycosylations performed by purified α-D-glucosidase of the marine mollusc Aplysia fasciata
    • Andreotti G., Giordano A., Tramice A., Mollo E., Trincone A. Hydrolyses and transglycosylations performed by purified α-D-glucosidase of the marine mollusc Aplysia fasciata. J. Biotechnol. 2006, 122:274-284.
    • (2006) J. Biotechnol. , vol.122 , pp. 274-284
    • Andreotti, G.1    Giordano, A.2    Tramice, A.3    Mollo, E.4    Trincone, A.5
  • 2
    • 0026674130 scopus 로고
    • Sequence of the complete cDNA and the 5' structure of the human sucrase-isomaltase gene. Possible homology with a yeast
    • Chantret I., Lacasa M., Chevalier G., Ruf J., Islam I., Mantei N., Edwards Y., Swallow D., Rousset M. Sequence of the complete cDNA and the 5' structure of the human sucrase-isomaltase gene. Possible homology with a yeast. Biochem. J. 1992, 285:915-923.
    • (1992) Biochem. J. , vol.285 , pp. 915-923
    • Chantret, I.1    Lacasa, M.2    Chevalier, G.3    Ruf, J.4    Islam, I.5    Mantei, N.6    Edwards, Y.7    Swallow, D.8    Rousset, M.9
  • 3
    • 0002339053 scopus 로고
    • α-Glucosidases
    • Pergamon Press, Oxford, United Kingdom, Amylase Research Society of Japan (Ed.)
    • Chiba S. α-Glucosidases. Handbook of amylases and related enzymes 1988, 104-116. Pergamon Press, Oxford, United Kingdom. 1st ed. Amylase Research Society of Japan (Ed.).
    • (1988) Handbook of amylases and related enzymes , pp. 104-116
    • Chiba, S.1
  • 4
    • 0031201675 scopus 로고    scopus 로고
    • Molecular mechanism in α-glucosidase and glucoamylase
    • Chiba S. Molecular mechanism in α-glucosidase and glucoamylase. Biosci. Biotechnol. Biochem. 1997, 61:1233-1239.
    • (1997) Biosci. Biotechnol. Biochem. , vol.61 , pp. 1233-1239
    • Chiba, S.1
  • 6
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 1987, 162:156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 7
    • 0031972297 scopus 로고    scopus 로고
    • Plant α-glucosidases of the glycoside hydrolase family 31. Molecular properties, substrate specificity, reaction mechanism, and comparison with family members of different origin
    • Frandsen T.P., Svensson B. Plant α-glucosidases of the glycoside hydrolase family 31. Molecular properties, substrate specificity, reaction mechanism, and comparison with family members of different origin. Plant Mol. Biol. 1998, 37:1-13.
    • (1998) Plant Mol. Biol. , vol.37 , pp. 1-13
    • Frandsen, T.P.1    Svensson, B.2
  • 8
    • 0026571574 scopus 로고
    • Starch digestion and absorption in nonruminants
    • Gray G.M. Starch digestion and absorption in nonruminants. J. Nutr. 1992, 122:172-177.
    • (1992) J. Nutr. , vol.122 , pp. 172-177
    • Gray, G.M.1
  • 9
    • 0024026526 scopus 로고
    • Primary structure and processing of lysosomal α-glucosidase; homology with the intestinal sucrase-isomaltase complex
    • Hoefsloot L.H., Hoogeveen-Westerveld M., Kroos M.A., van Beeumen J., Reuser A.J., Oostra B.A. Primary structure and processing of lysosomal α-glucosidase; homology with the intestinal sucrase-isomaltase complex. EMBO J. 1988, 7:1697-1704.
    • (1988) EMBO J. , vol.7 , pp. 1697-1704
    • Hoefsloot, L.H.1    Hoogeveen-Westerveld, M.2    Kroos, M.A.3    van Beeumen, J.4    Reuser, A.J.5    Oostra, B.A.6
  • 10
    • 67649964282 scopus 로고    scopus 로고
    • Enzymatic properties and the primary structure of a β-1,3-glucanase from the digestive fluid of the Pacific abalone Haliotis discus hannai
    • Kumagai Y., Ojima T. Enzymatic properties and the primary structure of a β-1,3-glucanase from the digestive fluid of the Pacific abalone Haliotis discus hannai. Comp. Biochem. Physiol. B 2009, 154:113-120.
    • (2009) Comp. Biochem. Physiol. B , vol.154 , pp. 113-120
    • Kumagai, Y.1    Ojima, T.2
  • 11
    • 84875256870 scopus 로고    scopus 로고
    • Enzymatic properties and the primary structure of two α-amylase isozymes from the Pacific abalone Haliotis discus hannai
    • Kumagai Y., Satoh T., Inoue A., Ojima T. Enzymatic properties and the primary structure of two α-amylase isozymes from the Pacific abalone Haliotis discus hannai. Comp. Biochem. Physiol. B 2013, 164:80-88.
    • (2013) Comp. Biochem. Physiol. B , vol.164 , pp. 80-88
    • Kumagai, Y.1    Satoh, T.2    Inoue, A.3    Ojima, T.4
  • 12
    • 0031593172 scopus 로고    scopus 로고
    • Molecular cloning of acid α-glucosidase cDNA of Japanese quail (Coturnix coturnix japonica) and the lack of its mRNA in acid maltase deficient quails
    • Kunita R., Nakabayashi O., Wu J.Y., Hagiwara Y., Mizutani M., Pennybacker M., Chen Y.T., Kikuchi T. Molecular cloning of acid α-glucosidase cDNA of Japanese quail (Coturnix coturnix japonica) and the lack of its mRNA in acid maltase deficient quails. Biochim. Biophys. Acta 1998, 1362:269-278.
    • (1998) Biochim. Biophys. Acta , vol.1362 , pp. 269-278
    • Kunita, R.1    Nakabayashi, O.2    Wu, J.Y.3    Hagiwara, Y.4    Mizutani, M.5    Pennybacker, M.6    Chen, Y.T.7    Kikuchi, T.8
  • 14
    • 0032579520 scopus 로고    scopus 로고
    • Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase
    • Nichols B.L., Eldering J., Avery S., Hahn D., Quaroni A., Sterchi E. Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase. J. Biol. Chem. 1998, 273:3076-3081.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3076-3081
    • Nichols, B.L.1    Eldering, J.2    Avery, S.3    Hahn, D.4    Quaroni, A.5    Sterchi, E.6
  • 15
    • 59349092050 scopus 로고    scopus 로고
    • Molecular characterization, gene expression analysis and biochemical properties of α-amylase from the disk abalone, Haliotis discus discus
    • Nikapitiya C., Oh C., Whang I., Kim C.G., Lee Y.H., Kim S.J., Lee J. Molecular characterization, gene expression analysis and biochemical properties of α-amylase from the disk abalone, Haliotis discus discus. Comp. Biochem. Physiol. B 2009, 152:271-281.
    • (2009) Comp. Biochem. Physiol. B , vol.152 , pp. 271-281
    • Nikapitiya, C.1    Oh, C.2    Whang, I.3    Kim, C.G.4    Lee, Y.H.5    Kim, S.J.6    Lee, J.7
  • 16
    • 33746915751 scopus 로고    scopus 로고
    • Isolation and cloning of an endo-β-1,4-mannanase from pacific abalone Haliotis discus hannai
    • Ootsuka S., Saga N., Suzuki K., Inoue A., Ojima T. Isolation and cloning of an endo-β-1,4-mannanase from pacific abalone Haliotis discus hannai. J. Biotechnol. 2006, 125:269-280.
    • (2006) J. Biotechnol. , vol.125 , pp. 269-280
    • Ootsuka, S.1    Saga, N.2    Suzuki, K.3    Inoue, A.4    Ojima, T.5
  • 17
    • 0017342054 scopus 로고
    • Improved resolution of myofibrillar proteins with sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • Porzio M.A., Pearson A.M. Improved resolution of myofibrillar proteins with sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Biochim. Biophys. Acta 1977, 490:27-34.
    • (1977) Biochim. Biophys. Acta , vol.490 , pp. 27-34
    • Porzio, M.A.1    Pearson, A.M.2
  • 18
    • 0344737824 scopus 로고    scopus 로고
    • CDNA cloning of an alginate lyase from abalone, Haliotis discus hannai
    • Shimizu E., Ojima T., Nishita K. cDNA cloning of an alginate lyase from abalone, Haliotis discus hannai. Carbohydr. Res. 2003, 328:2841-2852.
    • (2003) Carbohydr. Res. , vol.328 , pp. 2841-2852
    • Shimizu, E.1    Ojima, T.2    Nishita, K.3
  • 19
    • 0037294860 scopus 로고    scopus 로고
    • Purification and cDNA cloning of a cellulase from abalone Haliotis discus hannai
    • Suzuki K., Ojima T., Nishita K. Purification and cDNA cloning of a cellulase from abalone Haliotis discus hannai. Eur. J. Biochem. 2003, 270:771-778.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 771-778
    • Suzuki, K.1    Ojima, T.2    Nishita, K.3
  • 20
    • 33744982423 scopus 로고    scopus 로고
    • A novel oligoalginate lyase from abalone, Haliotis discus hannai, that releases disaccharide from alginate polymer in an exolytic manner
    • Suzuki H., Suzuki K., Inoue A., Ojima T. A novel oligoalginate lyase from abalone, Haliotis discus hannai, that releases disaccharide from alginate polymer in an exolytic manner. Carbohydr. Res. 2006, 341:1809-1819.
    • (2006) Carbohydr. Res. , vol.341 , pp. 1809-1819
    • Suzuki, H.1    Suzuki, K.2    Inoue, A.3    Ojima, T.4
  • 21
    • 77956920102 scopus 로고
    • Academic Press, New York, P. Boyer (Ed.)
    • Thoma J.A., Spradlin J.E., Dygert S. The Enzymes 1971, vol. 5:115-189. Academic Press, New York. third ed. P. Boyer (Ed.).
    • (1971) The Enzymes , vol.5 , pp. 115-189
    • Thoma, J.A.1    Spradlin, J.E.2    Dygert, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.