Isolation and properties of AMP deaminase from jumbo squid (Dosidicus gigas) mantle muscle from the Gulf of California,Mexico |
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Authors: | E Marquez-Rios R Pacheco-Aguilar FJ Castillo-Yañez CG Figueroa-Soto JM Ezquerra-Brauer T Gollas-Galvan |
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Affiliation: | 1. Centro de Investigación en Alimentación y Desarrollo, A.C. P.O. Box 1735, Hermosillo, Sonora 83000, Mexico;2. Departamento de Ciencias Químico Biológicas, Universidad de Sonora, Encinas y Rosales s/n, Hermosillo, Sonora 83000, Mexico |
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Abstract: | Adenosine monophosphate (AMP) deaminase was purified from jumbo squid mantle muscle by chromatography in cellulose phosphate, Q-Fast and 5′-AMP sepharose. Specific activity of 2.5 U/mg protein, 4.5% recovery and 133.68 purification fold were obtained at the end of the experiment. SDS–PAGE showed a single band with 87 kDa molecular mass, native PAGE proved a band of 178 kDa, whereas gel filtration detected a 180 kDa protein, suggesting the homodimeric nature of this enzyme, in which subunits are not linked by covalent forces. Isoelectric focusing of this enzyme showed a pI of 5.76, which agrees with pI values of AMP deaminase from other invertebrate organisms. AMP deaminase presented a kinetic sigmoidal plot with Vmax of 1.16 μM/min/mg, Km of 13 mM, Kcat of 3.48 μM.s−1 and a Kcat/Km of 267 (mol/L)−1.s−1. The apparent relative low catalytic activity of jumbo squid muscle AMP deaminase in the absence of positive effectors is similar to that reported for homologous enzymes in other invertebrate organisms. |
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Keywords: | AMP deaminase Jumbo squid mantle Purification |
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