AMP-deaminase from hen stomach smooth muscle - physico-chemical properties of the enzyme

• Autorzy: Swieca A. , Rybakowska I. , Koryziak A. , Klimek J. , Kaletha K.
• Języki publikacji: EN

Abstrakty

EN

AMP-deaminase from hen stomach smooth muscle was isolated and physico-chemi­cal properties of the purified enzyme were investigated. The enzyme had an activity optimum at pH 6.5, and poorly deaminated the substrate analogues tested. At optimum pH (6.5), in the absence of regulatory ligands (control conditions), the enzyme manifested hyperbolic substrate-saturation kinetics with half-saturation constant GS0.5) of about 4.5 mM. Additions of adenine nucleotide effectors (ATP, ADP) activated the enzyme strongly at all the concentrations tested, diminishing sig­nificantly the value of S0.5 constant. In contrast, the regulatory effect of ortho­phosphate was variable, and depended on the orthophosphate concentration used. The molecular mass of the enzyme subunit determined in SDS/PAG electrophore­sis was about of 37 kDa. The obtained results suggest that in different types of hen muscle, similarly as in humans and rats, expression of AMP-deaminase is under the control of independent genes.

Słowa kluczowe

EN

physicochemical property; hen; enzyme; AMP-deaminase; smooth muscle

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2004
• Tom: 51
• Numer: 1
• Opis fizyczny: p.213-218,fig.,ref.

Twórcy

autor

Swieca A.

• Medical University of Gdansk, Debinki 1, 80-211 Gdansk, Poland

autor

Rybakowska I.

autor

Koryziak A.

autor

Klimek J.

autor

Kaletha K.

Bibliografia

• Bradford MM. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein-dye binding. Anal Biochem.; 72: 248-54.
• Chaney AL, Marbach EP. (1961) Modified reagents for determination of urea and ammonia. Clin Chem.; 8: 130-2.
• Chapman AG, Atkinson DE. (1973) Stabilization of the adenylate energy charge by the adenylate deaminase reaction. J Biol Chem.; 248: 8309-12.
• Kaletha K. (1983) Regulatory properties of 14-day embryo and adult hen skeletal muscle AMP deaminase. Biochim Biophys Acta.; 759: 99-107.
• Kaletha K. (1988) Molecular forms of pigeon skeletal muscle AMP deaminase. Acta Biochim Polon.; 35: 405-14.
• Kaletha K, Skladanowski A. (1979) Regulatory properties of rat heart AMP deaminase. Biochim Biophys Acta.; 568: 80-90.
• Kaletha K, Skladanowski A. (1984) Regulatory properties of 14 day embryo and adult hen heart AMP-deaminase. Int J Biochem.; 16: 75-81.
• Kaletha K, Bogdanowicz S, Raffin JP. (1987) Regulatory properties of pigeon heart muscle AMP deaminase. Biochimie.; 69: 117-23.
• Kaletha K, Skladanowski A, Bogdanowicz S, Zydowo M. (1979) Purification and some regulatory properties of human heart adenylate deaminase. Int J Biochem.; 10: 925-9.
• Makarewicz W, Stankiewicz A. (1974) AMP-aminohydrolase of human skeletal muscle. Partial purification and properties. Biochem Med.; 10: 180-97.
• Nagel-Starczynowska G, Nowak G, Kaletha K. (1991) Purification and properties of AMP-deaminase from human uterine smooth muscle. Biochim Biophys Acta.; 1073: 470-3.
• Ogasawara N, Goto H, Watanabe T. (1975) Isozymes of rat AMP deaminase. Biochim Biophys Acta.; 403: 530-7.
• Ogasawara N, Goto H, Yamada Y, Watanabe T, Asano T. (1982) AMP Deaminase isozymes in human tissues. Biochim Biophys Acta.; 714: 298-306.
• Sabina RL, Morisaki T, Clarke P, Eddy R, Shows TB, Morton CC, Holmes EW. (1990) Characterization of the human and rat myoadenylate deaminase genes. J Biol Chem.; 265: 9423-33.
• Sammons DW, Chilson OP. (1978) AMP-deaminase: stage-specific isozymes in differentiating chick muscle. Arch Biochem Biophys. ; 191: 561-70.
• Smiley KL, Berry AJ, Suelter CH. (1967) An improved purification, crystallization, and some properties of rabbit muscle 5'-adenylic acid deaminase. J Biol Chem.; 242: 2502-6.
• Stankiewicz A, Spychala J, Skladanowski A, Zydowo M. (1979) 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. Comp Biochem Physiol B.; 62: 363-9.