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Volumn 132, Issue , 2015, Pages 41-49

Enzymatic synthesis of 2-deoxyglucose-containing maltooligosaccharides for tracing the location of glucose absorption from starch digestion

Author keywords

2 Deoxyglucose (2 DG); Amylosucrase; Glucose absorption; Maltooligosaccharides; Mucosal glucosidases

Indexed keywords

LOCATION;

EID: 84934293380     PISSN: 01448617     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.carbpol.2015.06.012     Document Type: Article
Times cited : (9)

References (44)
  • 1
    • 80053407853 scopus 로고    scopus 로고
    • GLUT2 accumulation in enterocyte apical and intracellular membranes: A study in morbidly obese human subjects and ob/ob and high fat-fed mice
    • A. Ait-Omar, M. Monteiro-Sepulveda, C. Poitou, M. Le Gall, A. Cotillard, and J. Gilet GLUT2 accumulation in enterocyte apical and intracellular membranes: A study in morbidly obese human subjects and ob/ob and high fat-fed mice Diabetes 60 10 2011 2598 2607
    • (2011) Diabetes , vol.60 , Issue.10 , pp. 2598-2607
    • Ait-Omar, A.1    Monteiro-Sepulveda, M.2    Poitou, C.3    Le Gall, M.4    Cotillard, A.5    Gilet, J.6
  • 2
    • 0036796410 scopus 로고    scopus 로고
    • Rapid insertion of GLUT2 into the rat jejunal brush-border membrane promoted by glucagon-like peptide 2
    • A. Au, A. Gupta, P. Schembri, and C.I. Cheeseman Rapid insertion of GLUT2 into the rat jejunal brush-border membrane promoted by glucagon-like peptide 2 Biochemical Journal 367 1 2002 247 254
    • (2002) Biochemical Journal , vol.367 , Issue.1 , pp. 247-254
    • Au, A.1    Gupta, A.2    Schembri, P.3    Cheeseman, C.I.4
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Analytical Biochemistry 72 1/2 1976 248
    • (1976) Analytical Biochemistry , vol.72 , Issue.1-2 , pp. 248
    • Bradford, M.M.1
  • 4
    • 0026447087 scopus 로고
    • Mammalian facilitative glucose transporters: Evidence for similar substrate recognition sites in functionally monomeric proteins
    • C.F. Burant, and G.I. Bell Mammalian facilitative glucose transporters: Evidence for similar substrate recognition sites in functionally monomeric proteins Biochemistry 31 42 1992 10414 10420
    • (1992) Biochemistry , vol.31 , Issue.42 , pp. 10414-10420
    • Burant, C.F.1    Bell, G.I.2
  • 6
    • 0014443148 scopus 로고
    • Column chromatography of human small-intestinal maltase, isomaltase and invertase activities
    • A. Dahlqvist, and U. Telenius Column chromatography of human small-intestinal maltase, isomaltase and invertase activities Biochemical Journal 111 2 1969 139 146
    • (1969) Biochemical Journal , vol.111 , Issue.2 , pp. 139-146
    • Dahlqvist, A.1    Telenius, U.2
  • 7
    • 0021955445 scopus 로고
    • Functional organization in cortical barrels of normal and vibrissae-damaged mice: A (3H) 2-deoxyglucose study
    • D. Durham, and T.A. Woolsey Functional organization in cortical barrels of normal and vibrissae-damaged mice: A (3H) 2-deoxyglucose study Journal of Comparative Neurology 235 1 1985 97 110
    • (1985) Journal of Comparative Neurology , vol.235 , Issue.1 , pp. 97-110
    • Durham, D.1    Woolsey, T.A.2
  • 8
    • 0004191820 scopus 로고    scopus 로고
    • McGraw-Hill, College New York, NY
    • S.I. Fox Human Physiology 2004 McGraw-Hill College New York, NY
    • (2004) Human Physiology
    • Fox, S.I.1
  • 9
    • 0018166544 scopus 로고
    • Metabolic trapping as a principle of radiopharmaceutical design: Some factors responsible for the biodistribution of [18F] 2-deoxy-2-fluoro-d-glucose
    • B.M. Gallagher, J.S. Fowler, N.I. Gutterson, R.R. MacGregor, C.-N. Wan, and A.P. Wolf Metabolic trapping as a principle of radiopharmaceutical design: Some factors responsible for the biodistribution of [18F] 2-deoxy-2-fluoro-d-glucose Journal of Nuclear Medicine 19 10 1978 1154 1161
    • (1978) Journal of Nuclear Medicine , vol.19 , Issue.10 , pp. 1154-1161
    • Gallagher, B.M.1    Fowler, J.S.2    Gutterson, N.I.3    MacGregor, R.R.4    Wan, C.-N.5    Wolf, A.P.6
  • 11
    • 0029281599 scopus 로고
    • Human small intestinal sucrase-isomaltase: Different binding patterns for malto- and isomaltooligosaccharides
    • H. Heymann, D. Breitmeier, and S. Günther Human small intestinal sucrase-isomaltase: Different binding patterns for malto- and isomaltooligosaccharides Biological Chemistry Hoppe-Seyler 376 4 1995 249 253
    • (1995) Biological Chemistry Hoppe-Seyler , vol.376 , Issue.4 , pp. 249-253
    • Heymann, H.1    Breitmeier, D.2    Günther, S.3
  • 12
    • 0028466976 scopus 로고
    • Calculation of subsite affinities of human small intestinal glucoamylase-maltase
    • H. Heymann, and S. Günther Calculation of subsite affinities of human small intestinal glucoamylase-maltase Biological Chemistry Hoppe-Seyler 375 7 1994 451 455
    • (1994) Biological Chemistry Hoppe-Seyler , vol.375 , Issue.7 , pp. 451-455
    • Heymann, H.1    Günther, S.2
  • 13
    • 0021042537 scopus 로고
    • Glucose absorption from starch hydrolysates in the human jejunum
    • B.J. Jones, B.E. Brown, J.S. Loran, D. Edgerton, J.F. Kennedy, and J.A. Stead Glucose absorption from starch hydrolysates in the human jejunum Gut 24 12 1983 1152 1160
    • (1983) Gut , vol.24 , Issue.12 , pp. 1152-1160
    • Jones, B.J.1    Brown, B.E.2    Loran, J.S.3    Edgerton, D.4    Kennedy, J.F.5    Stead, J.A.6
  • 14
    • 79959518480 scopus 로고    scopus 로고
    • Mapping the intestinal alpha-glucogenic enzyme specificities of starch digesting maltase-glucoamylase and sucrase-isomaltase
    • K. Jones, L. Sim, S. Mohan, J. Kumarasamy, H. Liu, and S. Avery Mapping the intestinal alpha-glucogenic enzyme specificities of starch digesting maltase-glucoamylase and sucrase-isomaltase Bioorganic & Medicinal Chemistry 19 13 2011 3929 3934
    • (2011) Bioorganic & Medicinal Chemistry , vol.19 , Issue.13 , pp. 3929-3934
    • Jones, K.1    Sim, L.2    Mohan, S.3    Kumarasamy, J.4    Liu, H.5    Avery, S.6
  • 15
    • 68949186622 scopus 로고    scopus 로고
    • Enzymatic synthesis of salicin glycosides through transglycosylation catalyzed by amylosucrases from Deinococcus geothermalis and Neisseria polysaccharea
    • J.-H. Jung, D.-H. Seo, S.-J. Ha, M.-C. Song, J. Cha, and S.-H. Yoo Enzymatic synthesis of salicin glycosides through transglycosylation catalyzed by amylosucrases from Deinococcus geothermalis and Neisseria polysaccharea Carbohydrate Research 344 13 2009 1612 1619
    • (2009) Carbohydrate Research , vol.344 , Issue.13 , pp. 1612-1619
    • Jung, J.-H.1    Seo, D.-H.2    Ha, S.-J.3    Song, M.-C.4    Cha, J.5    Yoo, S.-H.6
  • 16
    • 84873737849 scopus 로고    scopus 로고
    • Effects of amylosucrase treatment on molecular structure and digestion resistance of pre-gelatinised rice and barley starches
    • B.-S. Kim, H.-S. Kim, J.-S. Hong, K.C. Huber, J.-H. Shim, and S.-H. Yoo Effects of amylosucrase treatment on molecular structure and digestion resistance of pre-gelatinised rice and barley starches Food Chemistry 138 2/3 2013 966 975
    • (2013) Food Chemistry , vol.138 , Issue.2-3 , pp. 966-975
    • Kim, B.-S.1    Kim, H.-S.2    Hong, J.-S.3    Huber, K.C.4    Shim, J.-H.5    Yoo, S.-H.6
  • 17
    • 84925446594 scopus 로고    scopus 로고
    • Characterization of enzymatically modified rice and barley starches with amylosucrase at scale-up production
    • B.-S. Kim, H.-S. Kim, and S.-H. Yoo Characterization of enzymatically modified rice and barley starches with amylosucrase at scale-up production Carbohydrate Polymers 125 0 2015 61 68
    • (2015) Carbohydrate Polymers , vol.125 , pp. 61-68
    • Kim, B.-S.1    Kim, H.-S.2    Yoo, S.-H.3
  • 18
    • 79955697977 scopus 로고    scopus 로고
    • One-pot synthesis of cycloamyloses from sucrose by dual enzyme treatment: Combined reaction of amylosucrase and 4-α-glucanotransferase
    • J.-H. Kim, R. Wang, W.-H. Lee, C.-S. Park, S. Lee, and S.-H. Yoo One-pot synthesis of cycloamyloses from sucrose by dual enzyme treatment: Combined reaction of amylosucrase and 4-α-glucanotransferase Journal of Agricultural and Food Chemistry 59 9 2011 5044 5051
    • (2011) Journal of Agricultural and Food Chemistry , vol.59 , Issue.9 , pp. 5044-5051
    • Kim, J.-H.1    Wang, R.2    Lee, W.-H.3    Park, C.-S.4    Lee, S.5    Yoo, S.-H.6
  • 19
    • 0017170852 scopus 로고
    • 2-Deoxyglucose transport by intestinal epithelial cells isolated from the chick
    • G. Kimmich, and J. Randles 2-Deoxyglucose transport by intestinal epithelial cells isolated from the chick The Journal of Membrane Biology 27 1 1976 363 379
    • (1976) The Journal of Membrane Biology , vol.27 , Issue.1 , pp. 363-379
    • Kimmich, G.1    Randles, J.2
  • 21
    • 84875646353 scopus 로고    scopus 로고
    • Enzyme-synthesized highly branched maltodextrins have slow glucose generation at the mucosal α-glucosidase level and are slowly digestible in vivo
    • B.-H. Lee, L. Yan, R.J. Phillips, B.L. Reuhs, K. Jones, and D.R. Rose Enzyme-synthesized highly branched maltodextrins have slow glucose generation at the mucosal α-glucosidase level and are slowly digestible in vivo PLoS ONE 8 4 2013 e59745
    • (2013) PLoS ONE , vol.8 , Issue.4
    • Lee, B.-H.1    Yan, L.2    Phillips, R.J.3    Reuhs, B.L.4    Jones, K.5    Rose, D.R.6
  • 23
    • 84860439532 scopus 로고    scopus 로고
    • Unexpected high digestion rate of cooked starch by the ct-maltase-glucoamylase small intestine mucosal α-glucosidase subunit
    • A.H.-M. Lin, B.L. Nichols, R. Quezada-Calvillo, S.E. Avery, L. Sim, and D.R. Rose Unexpected high digestion rate of cooked starch by the ct-maltase-glucoamylase small intestine mucosal α-glucosidase subunit PLoS ONE 7 5 2012 e35473
    • (2012) PLoS ONE , vol.7 , Issue.5
    • Lin, A.H.-M.1    Nichols, B.L.2    Quezada-Calvillo, R.3    Avery, S.E.4    Sim, L.5    Rose, D.R.6
  • 25
    • 0035979360 scopus 로고    scopus 로고
    • Crystal structures of amylosucrase from Neisseria polysaccharea in complex with d-glucose and the active site mutant Glu328Gln in complex with the natural substrate sucrose
    • O. Mirza, L.K. Skov, M. Remaud-Simeon, G. Potocki de Montalk, C. Albenne, and P. Monsan Crystal structures of amylosucrase from Neisseria polysaccharea in complex with d-glucose and the active site mutant Glu328Gln in complex with the natural substrate sucrose Biochemistry 40 30 2001 9032 9039
    • (2001) Biochemistry , vol.40 , Issue.30 , pp. 9032-9039
    • Mirza, O.1    Skov, L.K.2    Remaud-Simeon, M.3    Potocki De Montalk, G.4    Albenne, C.5    Monsan, P.6
  • 26
    • 0023032374 scopus 로고
    • Infarct rim: Effect of hyperglycemia on direct current potential and [14C]2-deoxyglucose phosphorylation
    • M. Nedergaard, and J. Astrup Infarct rim: Effect of hyperglycemia on direct current potential and [14C]2-deoxyglucose phosphorylation Journal of Cerebral Blood Flow & Metabolism 6 5 1986 607 615
    • (1986) Journal of Cerebral Blood Flow & Metabolism , vol.6 , Issue.5 , pp. 607-615
    • Nedergaard, M.1    Astrup, J.2
  • 27
    • 0027928905 scopus 로고
    • Quantitative aspects of glucose and glutamine metabolism by intestinal cells
    • E.A. Newsholme, and A.L. Carrié Quantitative aspects of glucose and glutamine metabolism by intestinal cells Gut 35 1 Suppl. 1994 S13 S17
    • (1994) Gut , vol.35 , Issue.1 , pp. S13-S17
    • Newsholme, E.A.1    Carrié, A.L.2
  • 28
    • 70449345550 scopus 로고    scopus 로고
    • Merck & Co., Inc Whitehouse Station, NJ
    • M.J. O'Neil The Merck Index 2006 Merck & Co., Inc Whitehouse Station, NJ
    • (2006) The Merck Index
    • O'Neil, M.J.1
  • 29
    • 0017817786 scopus 로고
    • Mechanisms of the ability of insulin to activate the glucose-transport system in rat adipocytes
    • J.M. Olefsky Mechanisms of the ability of insulin to activate the glucose-transport system in rat adipocytes Biochemical Journal 172 1 1978 137 145
    • (1978) Biochemical Journal , vol.172 , Issue.1 , pp. 137-145
    • Olefsky, J.M.1
  • 30
    • 33751005820 scopus 로고    scopus 로고
    • The action mode of Thermus aquaticus YT-1 4-α-glucanotransferase and its chimeric enzymes introduced with starch-binding domain on amylose and amylopectin
    • J.-H. Park, H.-J. Kim, Y.-H. Kim, H. Cha, Y.-W. Kim, and T.-J. Kim The action mode of Thermus aquaticus YT-1 4-α-glucanotransferase and its chimeric enzymes introduced with starch-binding domain on amylose and amylopectin Carbohydrate Polymers 67 2 2007 164 173
    • (2007) Carbohydrate Polymers , vol.67 , Issue.2 , pp. 164-173
    • Park, J.-H.1    Kim, H.-J.2    Kim, Y.-H.3    Cha, H.4    Kim, Y.-W.5    Kim, T.-J.6
  • 36
    • 41549159900 scopus 로고    scopus 로고
    • Luminal starch substrate Brake on maltase-glucoamylase activity is located within the glucoamylase subunit
    • R. Quezada-Calvillo, L. Sim, Z. Ao, B.R. Hamaker, A. Quaroni, and G.D. Brayer Luminal starch substrate Brake on maltase-glucoamylase activity is located within the glucoamylase subunit Journal of Nutrition 138 4 2008 685 692
    • (2008) Journal of Nutrition , vol.138 , Issue.4 , pp. 685-692
    • Quezada-Calvillo, R.1    Sim, L.2    Ao, Z.3    Hamaker, B.R.4    Quaroni, A.5    Brayer, G.D.6
  • 37
    • 0030093952 scopus 로고    scopus 로고
    • Intestinal sodium-dependent d-glucose co-transporter: Dietary regulation
    • S.P. Shirazi-Beechey Intestinal sodium-dependent d-glucose co-transporter: Dietary regulation Proceedings of the Nutrition Society 55 1B 1996 167L 178
    • (1996) Proceedings of the Nutrition Society , vol.55 , Issue.1 , pp. 167L178
    • Shirazi-Beechey, S.P.1
  • 39
    • 0035949597 scopus 로고    scopus 로고
    • Normal kinetics of intestinal glucose absorption in the absence of GLUT2: Evidence for a transport pathway requiring glucose phosphorylation and transfer into the endoplasmic reticulum
    • F. Stümpel, R. Burcelin, K. Jungermann, and B. Thorens Normal kinetics of intestinal glucose absorption in the absence of GLUT2: Evidence for a transport pathway requiring glucose phosphorylation and transfer into the endoplasmic reticulum Proceedings of the National Academy of Sciences 98 20 2001 11330 11335
    • (2001) Proceedings of the National Academy of Sciences , vol.98 , Issue.20 , pp. 11330-11335
    • Stümpel, F.1    Burcelin, R.2    Jungermann, K.3    Thorens, B.4
  • 41
    • 77953069866 scopus 로고    scopus 로고
    • Enzymatic quantitation of total starch in plant products
    • R.E. Wrolstad, T.E. Acree, E.A. Decker, M.H. Penner, D.S. Reid, S.J. Schwartz, C.F. Shoemaker, D.M. Smith, P. Sporns, John Wiley & Sons, Inc Hoboken, NJ
    • T. Vasanthan Enzymatic quantitation of total starch in plant products R.E. Wrolstad, T.E. Acree, E.A. Decker, M.H. Penner, D.S. Reid, S.J. Schwartz, C.F. Shoemaker, D.M. Smith, P. Sporns, Current Protocols in Food Analytical Chemistry 2001 John Wiley & Sons, Inc Hoboken, NJ pp. E2.2.1-E2.2
    • (2001) Current Protocols in Food Analytical Chemistry , pp. E2.2.1-E2.2.2
    • Vasanthan, T.1
  • 42
    • 84855651173 scopus 로고    scopus 로고
    • Development of an efficient bioprocess for turanose production by sucrose isomerisation reaction of amylosucrase
    • R. Wang, J.-S. Bae, J.-H. Kim, B.-S. Kim, S.-H. Yoon, and C.-S. Park Development of an efficient bioprocess for turanose production by sucrose isomerisation reaction of amylosucrase Food Chemistry 132 2 2012 773 779
    • (2012) Food Chemistry , vol.132 , Issue.2 , pp. 773-779
    • Wang, R.1    Bae, J.-S.2    Kim, J.-H.3    Kim, B.-S.4    Yoon, S.-H.5    Park, C.-S.6
  • 44
    • 59249086077 scopus 로고    scopus 로고
    • PET and macro- and microautoradiographic studies combined with immunohistochemistry for monitoring rat intestinal ulceration and healing processes
    • M. Yamato, Y. Kataoka, H. Mizuma, Y. Wada, and Y. Watanabe PET and macro- and microautoradiographic studies combined with immunohistochemistry for monitoring rat intestinal ulceration and healing processes Journal of Nuclear Medicine 50 2 2009 266 273
    • (2009) Journal of Nuclear Medicine , vol.50 , Issue.2 , pp. 266-273
    • Yamato, M.1    Kataoka, Y.2    Mizuma, H.3    Wada, Y.4    Watanabe, Y.5


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