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Volumn 1430, Issue 2, 1999, Pages 281-289

Molecular cloning and primary structure analysis of porcine pancreatic α-amylase

Author keywords

Amylase form; cDNA library; Nested polymerase chain reaction; Nucleotide sequence; Peptidic sequence; Structural homology

Indexed keywords

AMYLASE;

EID: 0033062408     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(99)00011-4     Document Type: Article
Times cited : (26)

References (31)
  • 1
    • 0028021627 scopus 로고
    • Sequence similarities and evolutionary relationships of microbial, plant and animal α-amylase
    • Janecek S. Sequence similarities and evolutionary relationships of microbial, plant and animal α-amylase. Eur. J. Biochem. 224:1994;519-524.
    • (1994) Eur. J. Biochem. , vol.224 , pp. 519-524
    • Janecek, S.1
  • 3
    • 0016436566 scopus 로고
    • Enzymatic activity of TNB blocked porcine pancreatic α-amylase
    • Granger M., Abadie B., Mazzei Y., Marchis-Mouren G. Enzymatic activity of TNB blocked porcine pancreatic α-amylase. FEBS Lett. 50:1975;276-278.
    • (1975) FEBS Lett. , vol.50 , pp. 276-278
    • Granger, M.1    Abadie, B.2    Mazzei, Y.3    Marchis-Mouren, G.4
  • 4
    • 0029957475 scopus 로고    scopus 로고
    • The mechanism of porcine pancreatic α-amylase. Kinetic evidence for two additional carbohydrate-binding sites
    • Alkazaz M., Desseaux V., Marchis-Mouren G., Payan F., Forest E., Santimone M. The mechanism of porcine pancreatic α-amylase. Kinetic evidence for two additional carbohydrate-binding sites. Eur. J. Biochem. 241:1996;781-796.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 781-796
    • Alkazaz, M.1    Desseaux, V.2    Marchis-Mouren, G.3    Payan, F.4    Forest, E.5    Santimone, M.6
  • 5
    • 0028920217 scopus 로고
    • Subsite mapping of porcine pancreatic alpha-amylase I and II using p-nitrophenyl-α-maltooligosaccharides
    • Ajandouz E.H., Marchis-Mouren G. Subsite mapping of porcine pancreatic alpha-amylase I and II using p-nitrophenyl-α-maltooligosaccharides. Carbohydr. Res. 268:1995;267-277.
    • (1995) Carbohydr. Res. , vol.268 , pp. 267-277
    • Ajandouz, E.H.1    Marchis-Mouren, G.2
  • 6
    • 0019890472 scopus 로고
    • Amino acid sequence of hog pancreatic alpha-amylase isoenzyme I
    • Kluh I. Amino acid sequence of hog pancreatic alpha-amylase isoenzyme I. FEBS Lett. 136:1981;231-234.
    • (1981) FEBS Lett. , vol.136 , pp. 231-234
    • Kluh, I.1
  • 7
    • 0022629141 scopus 로고
    • Complete amino acid sequence and location of the five disulfide bridges in porcine pancreatic α-amylase
    • Pasero L., Mazzei Y., Abadie B., Chicheportiche Y., Marchis-Mouren G. Complete amino acid sequence and location of the five disulfide bridges in porcine pancreatic α-amylase. Biochim. Biophys. Acta. 869:1986;147-157.
    • (1986) Biochim. Biophys. Acta , vol.869 , pp. 147-157
    • Pasero, L.1    Mazzei, Y.2    Abadie, B.3    Chicheportiche, Y.4    Marchis-Mouren, G.5
  • 8
    • 0344948480 scopus 로고
    • Hog pancreatic α-amylase. Peptides from tryptic digest of isozyme AII
    • Meloun B., Kluh I., Moravek L. Hog pancreatic α-amylase. Peptides from tryptic digest of isozyme AII. Collection Czech. Chem. Commun. 45:1980;2572-2582.
    • (1980) Collection Czech. Chem. Commun. , vol.45 , pp. 2572-2582
    • Meloun, B.1    Kluh, I.2    Moravek, L.3
  • 9
    • 0027296794 scopus 로고
    • Structure and nuclear model refinement of pig pancreatic α-amylase I at 2.1 Å resolution
    • Qian M., Haser R., Payan F. Structure and nuclear model refinement of pig pancreatic α-amylase I at 2.1 Å resolution. J. Mol. Biol. 231:1993;785-9799.
    • (1993) J. Mol. Biol. , vol.231 , pp. 785-9799
    • Qian, M.1    Haser, R.2    Payan, F.3
  • 10
    • 0029953633 scopus 로고    scopus 로고
    • Crystal structure of pig pancreatic α-amylase isoenzyme II in complex with the carbohydrate inhibitor acarbose
    • Gilles C., Astier J.P., Marchis-Mouren G., Cambillau C., Payan F. Crystal structure of pig pancreatic α-amylase isoenzyme II in complex with the carbohydrate inhibitor acarbose. Eur. J. Biochem. 238:1996;561-569.
    • (1996) Eur. J. Biochem. , vol.238 , pp. 561-569
    • Gilles, C.1    Astier, J.P.2    Marchis-Mouren, G.3    Cambillau, C.4    Payan, F.5
  • 11
    • 0032520085 scopus 로고    scopus 로고
    • The mechanism of porcine pancreatic α-amylase. Inhibition of maltopentaose hydrolysis by acarbose maltose and maltotriose
    • Alkazaz M., Desseaux V., Marchis-Mouren G., Prodanov E., Santimone M. The mechanism of porcine pancreatic α-amylase. Inhibition of maltopentaose hydrolysis by acarbose maltose and maltotriose. Eur. J. Biochem. 243:1998;1-8.
    • (1998) Eur. J. Biochem. , vol.243 , pp. 1-8
    • Alkazaz, M.1    Desseaux, V.2    Marchis-Mouren, G.3    Prodanov, E.4    Santimone, M.5
  • 12
    • 0031442155 scopus 로고    scopus 로고
    • Characterization and functional properties of the α-amylase inhibitor (α-AI) from kidney bean (Phaseolus vulgaris) seeds
    • Le Berre-Anton V., Bompard-Gilles C., Payan F., Rougé P. Characterization and functional properties of the α-amylase inhibitor (α-AI) from kidney bean (Phaseolus vulgaris) seeds. Biochim. Biophys. Acta. 1343:1997;31-40.
    • (1997) Biochim. Biophys. Acta , vol.1343 , pp. 31-40
    • Le Berre-Anton, V.1    Bompard-Gilles, C.2    Payan, F.3    Rougé, P.4
  • 13
    • 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. 162:1987;156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 18
    • 0024234855 scopus 로고
    • CLUSTAL V: A package for performing multiple sequence alignment on a microcomputer
    • Higgins D.G., Sharp P.M. CLUSTAL V: a package for performing multiple sequence alignment on a microcomputer. Gene. 73:1988;237-244.
    • (1988) Gene , vol.73 , pp. 237-244
    • Higgins, D.G.1    Sharp, P.M.2
  • 19
    • 0344086513 scopus 로고
    • Hog pancreatic α-amylase; N-terminal sequence analysis
    • Kluh I. Hog pancreatic α-amylase; N-terminal sequence analysis. Collection Czech. Chem. Commun. 44:1979;145-147.
    • (1979) Collection Czech. Chem. Commun. , vol.44 , pp. 145-147
    • Kluh, I.1
  • 20
    • 0028966756 scopus 로고
    • Carbohydrate binding sites in a pancreatic α-amylase-substrate complex, derived from X-ray structure analysis at 2.1 Å resolution
    • Qian M., Haser R., Payan F. Carbohydrate binding sites in a pancreatic α-amylase-substrate complex, derived from X-ray structure analysis at 2.1 Å resolution. Protein Sci. 4:1995;747-755.
    • (1995) Protein Sci. , vol.4 , pp. 747-755
    • Qian, M.1    Haser, R.2    Payan, F.3
  • 21
    • 46149139867 scopus 로고
    • Corrected sequences of cDNAs for human salivary and pancreatic α-amylases
    • Nishide T., Emi M., Nakamura Y., Matsubara K. Corrected sequences of cDNAs for human salivary and pancreatic α-amylases. Gene. 50:1986;371-372.
    • (1986) Gene , vol.50 , pp. 371-372
    • Nishide, T.1    Emi, M.2    Nakamura, Y.3    Matsubara, K.4
  • 22
    • 0021728736 scopus 로고
    • Multiple non-allelic genes encoding pancreatic alpha-amylase of mouse are expressed in a strain-specific fashion
    • Tosi M., Bovey R., Astolfi S., Bodary S., Meisler M., Wellauer P.K. Multiple non-allelic genes encoding pancreatic alpha-amylase of mouse are expressed in a strain-specific fashion. EMBO J. 3:1984;2809-2816.
    • (1984) EMBO J. , vol.3 , pp. 2809-2816
    • Tosi, M.1    Bovey, R.2    Astolfi, S.3    Bodary, S.4    Meisler, M.5    Wellauer, P.K.6
  • 24
    • 0027497395 scopus 로고
    • 8-barrel enzymes revealed by conserved regions of α-amylase
    • 8-barrel enzymes revealed by conserved regions of α-amylase. FEBS Lett. 316:1993;23-26.
    • (1993) FEBS Lett. , vol.316 , pp. 23-26
    • Janecek, S.1
  • 25
    • 0028429952 scopus 로고
    • Protein engineering in the α-amylase family: Catalytic mechanism, substrate specificity, and stability
    • Svensson B. Protein engineering in the α-amylase family: catalytic mechanism, substrate specificity, and stability. Plant Mol. Biol. 25:1994;141-157.
    • (1994) Plant Mol. Biol. , vol.25 , pp. 141-157
    • Svensson, B.1
  • 26
    • 0028847185 scopus 로고
    • 8-barrel enzymes as a possible indicator of their evolutionary relatedness
    • 8-barrel enzymes as a possible indicator of their evolutionary relatedness. Protein Eng. 8:1995;809-813.
    • (1995) Protein Eng. , vol.8 , pp. 809-813
    • Janecek, S.1    Balaz, S.2
  • 27
    • 0029111443 scopus 로고
    • The structure of human pancreatic alpha-amylase at 1.8. Å resolution and comparisons with related enzymes
    • Brayer G.D., Luo Y., Withers S.G. The structure of human pancreatic alpha-amylase at 1.8. Å resolution and comparisons with related enzymes. Protein Sci. 4:1995;1730-1742.
    • (1995) Protein Sci. , vol.4 , pp. 1730-1742
    • Brayer, G.D.1    Luo, Y.2    Withers, S.G.3
  • 28
    • 0028198814 scopus 로고
    • The active center of a mammalian alpha-amylase. Structure of the complex of a pancreatic alpha-amylase with a carbohydrate inhibitor refined to 2.2-Å resolution
    • Qian M., Haser R., Buisson G., Duee E., Payan F. The active center of a mammalian alpha-amylase. Structure of the complex of a pancreatic alpha-amylase with a carbohydrate inhibitor refined to 2.2-Å resolution. Biochemistry. 33:1994;6284-6294.
    • (1994) Biochemistry , vol.33 , pp. 6284-6294
    • Qian, M.1    Haser, R.2    Buisson, G.3    Duee, E.4    Payan, F.5
  • 29
    • 0030589635 scopus 로고    scopus 로고
    • Substrate mimicry in the active center of a mammalian α-amylase: Structural analysis of an enzyme-inhibitor complex
    • Bompard-Gilles C., Rousseau P., Rougé P., Payan F. Substrate mimicry in the active center of a mammalian α-amylase: structural analysis of an enzyme-inhibitor complex. Structure. 4:1996;1441-1452.
    • (1996) Structure , vol.4 , pp. 1441-1452
    • Bompard-Gilles, C.1    Rousseau, P.2    Rougé, P.3    Payan, F.4
  • 30
    • 0028359337 scopus 로고
    • Refined molecular structure of pig pancreatic alpha-amylase at 2.1 Å resolution
    • Larson S.B., Greenwood A., Cascio D., Day J., McPherson A. Refined molecular structure of pig pancreatic alpha-amylase at 2.1 Å resolution. J. Mol. Biol. 235:1994;1560-1584.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1560-1584
    • Larson, S.B.1    Greenwood, A.2    Cascio, D.3    Day, J.4    McPherson, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.