메뉴 건너뛰기




Volumn 140, Issue 1, 2005, Pages 73-80

Carbohydrases in camel (Camelus dromedarius) pancreas. Purification and characterization of glucoamylase

Author keywords

Camel; Carbohydrases; Characterization; Glucoamylase; Pancreas; Purification; Ruminants; Amylase

Indexed keywords

2 DIETHYLAMINOETHANOL; ALPHA GLUCOSIDASE; AMYLASE; BETA AMYLASE; BETA GLUCOSIDASE; CARBOHYDRATE DERIVATIVE; DISACCHARIDASE; GLUCAN 1,4 ALPHA GLUCOSIDASE; GLYCOGEN; LACTASE; SEPHAROSE; STARCH; SUCRASE; TREHALASE;

EID: 11144351008     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpc.2004.09.019     Document Type: Article
Times cited : (9)

References (38)
  • 1
    • 11144351028 scopus 로고
    • Polysaccharidases of the camel (Camelus dromedarius) intestine and pancreas
    • M.O. Abdalla, M. Mutasem, and S. El-Katim Polysaccharidases of the camel (Camelus dromedarius) intestine and pancreas Comp. Biochem. Physiol., A 69 1981 429 436
    • (1981) Comp. Biochem. Physiol., a , vol.69 , pp. 429-436
    • Abdalla, M.O.1    Mutasem, M.2    El-Katim, S.3
  • 2
    • 0001879039 scopus 로고    scopus 로고
    • Purification and characterization of α-amylases from vine shoot inter-nodes
    • P. Berbezy, L. Laurent, and A. Maujean Purification and characterization of α-amylases from vine shoot inter-nodes Plant Physiol. Biochem. 34 1996 353 361
    • (1996) Plant Physiol. Biochem. , vol.34 , pp. 353-361
    • Berbezy, P.1    Laurent, L.2    Maujean, A.3
  • 3
    • 78651031122 scopus 로고
    • Enzymes of starch degradation and synthesis
    • P. Bernfeld Enzymes of starch degradation and synthesis Adv. Enzymol. 12 1951 379 428
    • (1951) Adv. Enzymol. , vol.12 , pp. 379-428
    • Bernfeld, P.1
  • 4
    • 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 Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0018771044 scopus 로고
    • A comparative study of glucose metabolism between the camel (Camelus deromedarius) and the sheep (Ovis ories)
    • L.G. Chandrasena, B. Emmanuel, and H. Gilanpour A comparative study of glucose metabolism between the camel (Camelus deromedarius) and the sheep (Ovis ories) Comp. Biochem. Physiol., A 62 1979 837 840
    • (1979) Comp. Biochem. Physiol., a , vol.62 , pp. 837-840
    • Chandrasena, L.G.1    Emmanuel, B.2    Gilanpour, H.3
  • 7
    • 85045825330 scopus 로고
    • Regulation of pancreatic exocrine secretion in ruminants: A review
    • W.J. Croom, L.S. Bull, and I.L. Taylor Regulation of pancreatic exocrine secretion in ruminants: a review J. Nutr. 122 1991 199 202
    • (1991) J. Nutr. , vol.122 , pp. 199-202
    • Croom, W.J.1    Bull, L.S.2    Taylor, I.L.3
  • 8
    • 78651153791 scopus 로고
    • Disc electrophoresis. Method and application to human serum proteins
    • B.J. Davis Disc electrophoresis. Method and application to human serum proteins Ann. N.Y. Acad. Sci. 121 1964 404 427
    • (1964) Ann. N.Y. Acad. Sci. , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 9
    • 84981835608 scopus 로고
    • Purification de l,invertase de levure
    • E.H. Fischer, and L. Kohtes Purification de l,invertase de levure Helv. Chim. Acta 34 1951 1123 1131
    • (1951) Helv. Chim. Acta , vol.34 , pp. 1123-1131
    • Fischer, E.H.1    Kohtes, L.2
  • 10
    • 0018174191 scopus 로고
    • Purification of rat intestinal maltase-glucoamylase and its anomalous dissociation either by heat or by low pH
    • P.R. Flanagan, and G.G. Forstner Purification of rat intestinal maltase-glucoamylase and its anomalous dissociation either by heat or by low pH Biochem. J. 173 1978 553 563
    • (1978) Biochem. J. , vol.173 , pp. 553-563
    • Flanagan, P.R.1    Forstner, G.G.2
  • 11
    • 77956986901 scopus 로고
    • Preparation of buffers for use in enzyme studies
    • S.P. Colowick N.O. Kaplan Academic Press New York
    • G. Gomori Preparation of buffers for use in enzyme studies S.P. Colowick N.O. Kaplan Methods in Enzymology 1955 Academic Press New York 138 146
    • (1955) Methods in Enzymology , pp. 138-146
    • Gomori, G.1
  • 13
    • 0345698653 scopus 로고    scopus 로고
    • Di- and oligosaccharide substrate specificities and subsite binding energies of pig intestinal glucoamylase-maltase
    • S. Gunther, and H. Heymann Di- and oligosaccharide substrate specificities and subsite binding energies of pig intestinal glucoamylase-maltase Arch. Biochem. Biophys. 354 1998 111 116
    • (1998) Arch. Biochem. Biophys. , vol.354 , pp. 111-116
    • Gunther, S.1    Heymann, H.2
  • 14
    • 0026604544 scopus 로고
    • Dietary influences on carbohydrases and small intestinal starch hydrolysis capacity in ruminants
    • D.L. Harmon Dietary influences on carbohydrases and small intestinal starch hydrolysis capacity in ruminants J. Nutr. 122 1992 203 210
    • (1992) J. Nutr. , vol.122 , pp. 203-210
    • Harmon, D.L.1
  • 15
    • 0014136757 scopus 로고
    • Intestinal carbohydrase activity and carbohydrate utilization in mature sheep
    • F.G. Hembry, M.C. Bell, and R.F. Hall Intestinal carbohydrase activity and carbohydrate utilization in mature sheep J. Nutr. 93 1967 175 181
    • (1967) J. Nutr. , vol.93 , pp. 175-181
    • Hembry, F.G.1    Bell, M.C.2    Hall, R.F.3
  • 16
    • 0002143068 scopus 로고
    • Haemostatic parameter in the camel (Camelus dromedarius) comparison with human
    • M.F. Hussein, A.K. Al-Moen, and A.M.A. Gader Haemostatic parameter in the camel (Camelus dromedarius) comparison with human Comp. Haematol. Int. 2 1992 92 96
    • (1992) Comp. Haematol. Int. , vol.2 , pp. 92-96
    • Hussein, M.F.1    Al-Moen, A.K.2    Gader, A.M.A.3
  • 17
    • 0029127279 scopus 로고
    • Characterization of partially purified α-glucosidase in the soluble fraction of bovine crystalline lens
    • A. Kamei, and O. Fujiyama Characterization of partially purified α-glucosidase in the soluble fraction of bovine crystalline lens Biol. Pharm. Bull. 18 1995 1133 1137
    • (1995) Biol. Pharm. Bull. , vol.18 , pp. 1133-1137
    • Kamei, A.1    Fujiyama, O.2
  • 18
    • 0025483773 scopus 로고
    • Influence of dietary forage and feed intake on carbohydrase activities and small intestinal morphology of calves
    • K.K. Kreikemeier, D.L. Harmon, J.P. Peters, K.L. Gross, C.K. Armendariz, and C.R. Krehbiel Influence of dietary forage and feed intake on carbohydrase activities and small intestinal morphology of calves J. Anim. Sci. 68 1990 2916 2929
    • (1990) J. Anim. Sci. , vol.68 , pp. 2916-2929
    • Kreikemeier, K.K.1    Harmon, D.L.2    Peters, J.P.3    Gross, K.L.4    Armendariz, C.K.5    Krehbiel, C.R.6
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0028359791 scopus 로고
    • Dromedary pancreatic lipase: Purification and structural properties
    • H. Mejdoub, J. Reinbolt, and K. Gargouri Dromedary pancreatic lipase: purification and structural properties Biochim. Biophys. Acta 1213 1994 119 126
    • (1994) Biochim. Biophys. Acta , vol.1213 , pp. 119-126
    • Mejdoub, H.1    Reinbolt, J.2    Gargouri, K.3
  • 21
    • 0020017399 scopus 로고
    • The level and distribution of disaccharidases in the camel (Camelus dromedarius) intestine
    • M. Mutasium, S. El-Khatim, and M.O. Abdalla The level and distribution of disaccharidases in the camel (Camelus dromedarius) intestine Comp. Biochem. Physiol., B 71 1982 199 204
    • (1982) Comp. Biochem. Physiol., B , vol.71 , pp. 199-204
    • Mutasium, M.1    El-Khatim, S.2    Abdalla, M.O.3
  • 22
    • 0032579520 scopus 로고    scopus 로고
    • Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase
    • B.L. Nichols, J. Eldering, A. Stephen, D. Hahn, A. Quaroni, and E. Sterchi Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase J. Biol. Chem. 273 1998 3076 3081
    • (1998) J. Biol. Chem. , vol.273 , pp. 3076-3081
    • Nichols, B.L.1    Eldering, J.2    Stephen, A.3    Hahn, D.4    Quaroni, A.5    Sterchi, E.6
  • 23
    • 0037417990 scopus 로고    scopus 로고
    • The maltase-glucoamylase gene: Common ancestry to sucrase-isomaltase with complementary starch digestion activities
    • B.L. Nichols, S. Avery, P. Sen, D.M. Wallow, D. Hahn, and E. Sterchi The maltase-glucoamylase gene: common ancestry to sucrase-isomaltase with complementary starch digestion activities Proc. Natl. Acad. Sci. U. S. A. 100 2003 1432 1437
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 1432-1437
    • Nichols, B.L.1    Avery, S.2    Sen, P.3    Wallow, D.M.4    Hahn, D.5    Sterchi, E.6
  • 24
    • 0024535931 scopus 로고
    • Single active site mechanism of rabbit liver acid α-glucosidase
    • S. Onodera, H. Matsui, and S. Chiba Single active site mechanism of rabbit liver acid α-glucosidase J. Biochem. 105 1989 611 618
    • (1989) J. Biochem. , vol.105 , pp. 611-618
    • Onodera, S.1    Matsui, H.2    Chiba, S.3
  • 26
    • 0020951423 scopus 로고
    • Studies on the intestinal disaccharidases of the pigeon: III. Separation, purification and properties of sucrase-isomaltase and maltase-glucoamylase
    • K. Prakash, S.D. Patil, and S.N. Hedge Studies on the intestinal disaccharidases of the pigeon: III. Separation, purification and properties of sucrase-isomaltase and maltase-glucoamylase Arch. Int. Physiol. Biochim. 91 1983 379 390
    • (1983) Arch. Int. Physiol. Biochim. , vol.91 , pp. 379-390
    • Prakash, K.1    Patil, S.D.2    Hedge, S.N.3
  • 28
    • 0030447078 scopus 로고    scopus 로고
    • Purification and characterization of cationic trypsin from the pancreas of the Arabian camel (Camelus dromedarius)
    • A. Rafiq, and G.S. Bailey Purification and characterization of cationic trypsin from the pancreas of the Arabian camel (Camelus dromedarius) Comp. Biochem. Physiol., B 115 1996 363 367
    • (1996) Comp. Biochem. Physiol., B , vol.115 , pp. 363-367
    • Rafiq, A.1    Bailey, G.S.2
  • 29
    • 77956991036 scopus 로고
    • Purification of α-amylases by precipitation of amylase-glycogen complexes
    • S.P. Colowick N.O. Kaplan Academic Press New York
    • M. Schramm, and A. Loyter Purification of α-amylases by precipitation of amylase-glycogen complexes S.P. Colowick N.O. Kaplan Methods in Enzymol 1966 Academic Press New York 533 537
    • (1966) Methods in Enzymol , pp. 533-537
    • Schramm, M.1    Loyter, A.2
  • 31
    • 0014321655 scopus 로고
    • Carbohydrase activities in the bovine digestive tract
    • R.C. Siddons Carbohydrase activities in the bovine digestive tract Biochem. J. 108 1968 839 844
    • (1968) Biochem. J. , vol.108 , pp. 839-844
    • Siddons, R.C.1
  • 32
    • 0020017399 scopus 로고
    • The level and distribution of disaccharidases in the camel (Camelus dromedarius) intestine
    • M.M. Sir El Khatim, and A.M. Osman The level and distribution of disaccharidases in the camel (Camelus dromedarius) intestine Comp. Biochem. Physiol., A 71 1982 199 204
    • (1982) Comp. Biochem. Physiol., a , vol.71 , pp. 199-204
    • Sir El Khatim, M.M.1    Osman, A.M.2
  • 33
    • 0020451814 scopus 로고
    • Amphilic pig intestinal microvillus maltase-glucoamylase. Structure and specificity
    • H. Sorensen, O. Noren, H. Sjostrom, and E.M. Danielsen Amphilic pig intestinal microvillus maltase-glucoamylase. Structure and specificity J. Biochem. 126 1982 559 568
    • (1982) J. Biochem. , vol.126 , pp. 559-568
    • Sorensen, H.1    Noren, O.2    Sjostrom, H.3    Danielsen, E.M.4
  • 34
    • 0030570989 scopus 로고    scopus 로고
    • Purification and characterization of α-glucosidase complex from the intestine of the frog, Rana japonica
    • Y. Takesue, and S. Takesue Purification and characterization of α-glucosidase complex from the intestine of the frog, Rana japonica Biochim. Biophys. Acta 1296 1996 152 158
    • (1996) Biochim. Biophys. Acta , vol.1296 , pp. 152-158
    • Takesue, Y.1    Takesue, S.2
  • 35
    • 0022577128 scopus 로고
    • Purification and characterization of two components of acid α-glucosidase from pig liver
    • K. Tashiro, T. Iwamasa, H. Kato, H. Ogata, and M. Anai Purification and characterization of two components of acid α-glucosidase from pig liver J. Biochem. 99 1986 693 701
    • (1986) J. Biochem. , vol.99 , pp. 693-701
    • Tashiro, K.1    Iwamasa, T.2    Kato, H.3    Ogata, H.4    Anai, M.5
  • 36
    • 0015106007 scopus 로고
    • A gross study of compartmentalized stomach of two new-world camelides, the lama and guanaco
    • A.P. Vallenas, J.P. Cummingd, and J.F. Munnel A gross study of compartmentalized stomach of two new-world camelides, the lama and guanaco J. Morph. 134 1971 399 424
    • (1971) J. Morph. , vol.134 , pp. 399-424
    • Vallenas, A.P.1    Cummingd, J.P.2    Munnel, J.F.3
  • 37
    • 0000745994 scopus 로고
    • Isolation and crystallization of enolase
    • O. Warburg, and W. Christian Isolation and crystallization of enolase Biochem. Z. 310 1942 386 421
    • (1942) Biochem. Z. , vol.310 , pp. 386-421
    • Warburg, O.1    Christian, W.2
  • 38
    • 0016835868 scopus 로고
    • The amino acid sequence of dromedary pancreatic ribonuclease
    • K.D. Welling, G. Groen, and J.J. Beintema The amino acid sequence of dromedary pancreatic ribonuclease Biochem. J. 147 1975 505 551
    • (1975) Biochem. J. , vol.147 , pp. 505-551
    • Welling, K.D.1    Groen, G.2    Beintema, J.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.