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Volumn 110, Issue 1, 2008, Pages 69-75

Isolation and properties of AMP deaminase from jumbo squid (Dosidicus gigas) mantle muscle from the Gulf of California, Mexico

Author keywords

AMP deaminase; Jumbo squid mantle; Purification

Indexed keywords

ADENOSINE MONOPHOSPHATE DEAMINASE; ADENOSINE PHOSPHATE; CELLULOSE PHOSPHATE; HOMODIMER; SEPHAROSE;

EID: 41549142596     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodchem.2008.01.059     Document Type: Article
Times cited : (9)

References (30)
  • 1
    • 0017278611 scopus 로고
    • Subunit structure of AMP-deaminase from chicken and rabbit skeletal muscle
    • Boosman A., and Chilson O.P. Subunit structure of AMP-deaminase from chicken and rabbit skeletal muscle. Journal of Biological Chemistry 251 (1976) 1847-1852
    • (1976) Journal of Biological Chemistry , vol.251 , pp. 1847-1852
    • Boosman, A.1    Chilson, O.P.2
  • 2
    • 0017184389 scopus 로고
    • A Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of dye binding
    • Bradford M. A Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of dye binding. Analytical Biochemistry 72 (1976) 248-254
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.1
  • 3
    • 0017329916 scopus 로고
    • + and adenylate energy charge in expression of kinetic and regulatory properties
    • + and adenylate energy charge in expression of kinetic and regulatory properties. Journal of Biological Chemistry 252 (1977) 1606-1616
    • (1977) Journal of Biological Chemistry , vol.252 , pp. 1606-1616
    • Coffee, C.J.1    Solano, C.2
  • 8
    • 0023071917 scopus 로고
    • Activies of adenylate-degrading enzymes in muscle from vertebrates and invertebrates
    • Fujisawa K., and Yoshino M. Activies of adenylate-degrading enzymes in muscle from vertebrates and invertebrates. Comparative Biochemistry and Physiology 86 (1987) 109-112
    • (1987) Comparative Biochemistry and Physiology , vol.86 , pp. 109-112
    • Fujisawa, K.1    Yoshino, M.2
  • 9
    • 0037297179 scopus 로고    scopus 로고
    • Expresión, purification and inhibition of in vitro proteolysis of human AMPD2 (isoform L) recombinant enzymes
    • Haas A.M., and Sabina R.L. Expresión, purification and inhibition of in vitro proteolysis of human AMPD2 (isoform L) recombinant enzymes. Protein Expression and Purification 27 (2003) 293-303
    • (2003) Protein Expression and Purification , vol.27 , pp. 293-303
    • Haas, A.M.1    Sabina, R.L.2
  • 10
    • 0038028827 scopus 로고    scopus 로고
    • N-terminal extensions of the human AMPD2 polypeptide influence ATP regulation of isoform L
    • Haas A.M., and Sabina R.L. N-terminal extensions of the human AMPD2 polypeptide influence ATP regulation of isoform L. Biochemical and Biophysical Research Communications 305 (2003) 421-427
    • (2003) Biochemical and Biophysical Research Communications , vol.305 , pp. 421-427
    • Haas, A.M.1    Sabina, R.L.2
  • 11
    • 0007149804 scopus 로고
    • Accelerated nucleotide degradation and glycolysis during warming to and subsequent storage at -5 C of prerigor quick-frozen adductor muscle of the sea scallop (Placopecten magellanicus)
    • Hiltz D.F., Bishop L.J., and Dyer W.J. Accelerated nucleotide degradation and glycolysis during warming to and subsequent storage at -5 C of prerigor quick-frozen adductor muscle of the sea scallop (Placopecten magellanicus). Journal of the Fisheries Research Board of Canada 31 (1974) 1181-1187
    • (1974) Journal of the Fisheries Research Board of Canada , vol.31 , pp. 1181-1187
    • Hiltz, D.F.1    Bishop, L.J.2    Dyer, W.J.3
  • 12
    • 84872892311 scopus 로고    scopus 로고
    • Ibarra, L. L. R. (2006). Efectos sobre la calidad y funcionalidad del músculo de manto de calamar gigante (Dosidicus gigas) sometido al almacenamiento en hielo. Bachelor thesis. Centro de Investigación en Alimentación y Desarrollo, A.C. Hermosillo, Sonora, México.
    • Ibarra, L. L. R. (2006). Efectos sobre la calidad y funcionalidad del músculo de manto de calamar gigante (Dosidicus gigas) sometido al almacenamiento en hielo. Bachelor thesis. Centro de Investigación en Alimentación y Desarrollo, A.C. Hermosillo, Sonora, México.
  • 13
    • 0023851957 scopus 로고
    • Developmental forms of human skeletal-muscle AMP deaminase the kinetic and regulatory properties of the enzyme
    • Kaletha K., and Nowak G. Developmental forms of human skeletal-muscle AMP deaminase the kinetic and regulatory properties of the enzyme. Biochemical Journal 249 (1988) 255-261
    • (1988) Biochemical Journal , vol.249 , pp. 255-261
    • Kaletha, K.1    Nowak, G.2
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head bacteriophague T4
    • Laemmli U.K. Cleavage of structural proteins during assembly of the head bacteriophague T4. Nature 227 (1970) 680
    • (1970) Nature , vol.227 , pp. 680
    • Laemmli, U.K.1
  • 15
    • 0018412702 scopus 로고
    • Aspect of purine metabolism in the gill epithelium of rainbow trout, Salmo gairdneri richarson
    • Leray C., Raffin J.P., and Winninger C. Aspect of purine metabolism in the gill epithelium of rainbow trout, Salmo gairdneri richarson. Comparative Biochemistry and Physiology 62B (1979) 31-40
    • (1979) Comparative Biochemistry and Physiology , vol.62 B , pp. 31-40
    • Leray, C.1    Raffin, J.P.2    Winninger, C.3
  • 16
    • 0031879185 scopus 로고    scopus 로고
    • AMP-deaminase from sea scorpion white muscle: Properties and redistribution under hypoxia
    • Lushchak V.I., Smirnova Y.D., and Storey K.B. AMP-deaminase from sea scorpion white muscle: Properties and redistribution under hypoxia. Comparative Biochemistry and Physiology 119 (1998) 611-618
    • (1998) Comparative Biochemistry and Physiology , vol.119 , pp. 611-618
    • Lushchak, V.I.1    Smirnova, Y.D.2    Storey, K.B.3
  • 17
    • 34548494148 scopus 로고    scopus 로고
    • Postmortem biochemical behaviour of giant squid (Dosidicus gigas) mantle muscle stored in ice and its relation with quality parameters
    • Marquez-Rios E., Morán-Palacio E.F., Lugo-Sánchez M.E., Ocano-Higuera V.M., and Pacheco-Aguilar R. Postmortem biochemical behaviour of giant squid (Dosidicus gigas) mantle muscle stored in ice and its relation with quality parameters. Journal of Food Science 72 7 (2007) 356-362
    • (2007) Journal of Food Science , vol.72 , Issue.7 , pp. 356-362
    • Marquez-Rios, E.1    Morán-Palacio, E.F.2    Lugo-Sánchez, M.E.3    Ocano-Higuera, V.M.4    Pacheco-Aguilar, R.5
  • 18
    • 0035847035 scopus 로고    scopus 로고
    • Regulation of skeletal muscle AMP deaminase: Lisien residues are critical for the pH-dependent positive homotropic cooperativity behaviour of the rabbit enzyme
    • Martini A., Ranieri-Raggi M., Antonietta R.M., and Raggi S.A. Regulation of skeletal muscle AMP deaminase: Lisien residues are critical for the pH-dependent positive homotropic cooperativity behaviour of the rabbit enzyme. Biochimica et Biophysica Acta 1544 (2001) 123-132
    • (2001) Biochimica et Biophysica Acta , vol.1544 , pp. 123-132
    • Martini, A.1    Ranieri-Raggi, M.2    Antonietta, R.M.3    Raggi, S.A.4
  • 19
    • 0024790863 scopus 로고
    • Role in AMP degradation, large scale purification, and properties of the native and proteolyzed enzyme
    • Merkler D.J., Wali A.S., Taylor J., and Schramm V.L. Role in AMP degradation, large scale purification, and properties of the native and proteolyzed enzyme. Journal of Biological Chemistry 264 35 (1989) 21422-21430
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.35 , pp. 21422-21430
    • Merkler, D.J.1    Wali, A.S.2    Taylor, J.3    Schramm, V.L.4
  • 22
    • 0038128250 scopus 로고    scopus 로고
    • Ecto 5′-nucleotidase and nonspecific alkaline phosphatase. Two AMP-hidrolyzin ectoenzimes with distinct roles in human airways
    • Picher M., Burch L.H., Hirsh A.J., Spychala J., and Boucher R.C. Ecto 5′-nucleotidase and nonspecific alkaline phosphatase. Two AMP-hidrolyzin ectoenzimes with distinct roles in human airways. Journal of Biological Chemistry 278 (2003) 13468-13479
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 13468-13479
    • Picher, M.1    Burch, L.H.2    Hirsh, A.J.3    Spychala, J.4    Boucher, R.C.5
  • 23
    • 0037474256 scopus 로고    scopus 로고
    • Isolation by zinc-affinity chromatography of the histidine-proline-rich-glycoprotein molecula associated with rabbit skeletal muscle AMP deaminase. Evidence that the formation of protein-protein complex between the catalytic subunit and the novel component is critical for the stability of the enzyme
    • Ranieri-Raggi M., Martini D., Sabbatini A.R.M., Moir A.J.G., and Raggi A. Isolation by zinc-affinity chromatography of the histidine-proline-rich-glycoprotein molecula associated with rabbit skeletal muscle AMP deaminase. Evidence that the formation of protein-protein complex between the catalytic subunit and the novel component is critical for the stability of the enzyme. Biochimica et Biophysica Acta 1645 (2003) 81-88
    • (2003) Biochimica et Biophysica Acta , vol.1645 , pp. 81-88
    • Ranieri-Raggi, M.1    Martini, D.2    Sabbatini, A.R.M.3    Moir, A.J.G.4    Raggi, A.5
  • 24
    • 0014216746 scopus 로고
    • An improved purification, crystallization, and some properties of rabbit muscle 5′-adenylic acid deaminase
    • Smiley K.L., Berry A.J., and Suelter C.H. An improved purification, crystallization, and some properties of rabbit muscle 5′-adenylic acid deaminase. Journal of Biological Chemistry 242 (1967) 2502-2506
    • (1967) Journal of Biological Chemistry , vol.242 , pp. 2502-2506
    • Smiley, K.L.1    Berry, A.J.2    Suelter, C.H.3
  • 25
    • 41549108550 scopus 로고
    • Comparative studies on AMP-deaminase-IV. Amino acid composition of the enzymes from rat, rabbit, hen, frog, pikeperch skeletal muscle and frog liver
    • Stankiewicz A., and Spychala J. Comparative studies on AMP-deaminase-IV. Amino acid composition of the enzymes from rat, rabbit, hen, frog, pikeperch skeletal muscle and frog liver. Comparative Biochemistry and Physiology 69B (1981) 5-8
    • (1981) Comparative Biochemistry and Physiology , vol.69 B , pp. 5-8
    • Stankiewicz, A.1    Spychala, J.2
  • 26
    • 9344267225 scopus 로고
    • Comparative studies on AMP-deaminase VII. Purification and some properties of the enzyme from crayfish Orconectes Limosus tail muscle
    • Stankiewicz A. Comparative studies on AMP-deaminase VII. Purification and some properties of the enzyme from crayfish Orconectes Limosus tail muscle. Comparative Biochemistry and Physiology 72 (1982) 127-132
    • (1982) Comparative Biochemistry and Physiology , vol.72 , pp. 127-132
    • Stankiewicz, A.1
  • 27
    • 0018345761 scopus 로고
    • Comparative studies on muscle AMP-deaminase-I. Purification, molecular weight, subunit structure and metal content of the enzymes from rat, rabbit, hen, frog and pikeperch
    • Stankiewicz A., Spychala J., Skladanowski A.C., and Zydowo M. Comparative studies on muscle AMP-deaminase-I. Purification, molecular weight, subunit structure and metal content of the enzymes from rat, rabbit, hen, frog and pikeperch. Comparative Biochemistry and Physiology 62B (1979) 363-369
    • (1979) Comparative Biochemistry and Physiology , vol.62 B , pp. 363-369
    • Stankiewicz, A.1    Spychala, J.2    Skladanowski, A.C.3    Zydowo, M.4
  • 28
    • 2342573464 scopus 로고    scopus 로고
    • AMP-deaminase from hen stomach smooth muscle-physico-chemical properties of the enzyme
    • Swieca A., Rybakowska I., Koryziak A., Klimek J., and Kaletha K. AMP-deaminase from hen stomach smooth muscle-physico-chemical properties of the enzyme. Acta Biochimica Polonica 51 (2004) 213-218
    • (2004) Acta Biochimica Polonica , vol.51 , pp. 213-218
    • Swieca, A.1    Rybakowska, I.2    Koryziak, A.3    Klimek, J.4    Kaletha, K.5
  • 29
    • 0027499032 scopus 로고
    • Isolation and characterization of AMP deaminase from mammalian (rabbit) myocardium
    • Thakkar J.K., Janero D.R., Yarwod C., Sharif H., and Hreniuk D. Isolation and characterization of AMP deaminase from mammalian (rabbit) myocardium. Biochemical Journal 290 (1993) 335-341
    • (1993) Biochemical Journal , vol.290 , pp. 335-341
    • Thakkar, J.K.1    Janero, D.R.2    Yarwod, C.3    Sharif, H.4    Hreniuk, D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.