کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1975940 | 1060665 | 2009 | 7 صفحه PDF | دانلود رایگان |
Arginine kinase (AK) plays an important role in cellular energy metabolism in invertebrate. The encoding AK gene from Shrimp Metapenaeus ensis (M. ensis) was cloned in prokaryotic expression plasmid pET-28a, and it was then expressed in Escherichia coil in dissoluble form. The recombinant protein was purified by following three chromatography steps in turn: CM-Cellulose cation-exchange, Sephacryl S-100HR gel filtrate and DEAE-Sepharose anion-exchange. The purified AK’s apparent Km was 2.33 ± 0.1 and 1.59 ± 0.2 mM for ATP and l-arginine, respectively, while its optimum pH and temperature was 8.5 and 30 °C in the process of forward reaction, respectively. Phylogenetic analysis of cDNA-derived amino acid sequences for the AKs indicated a close affinity of M. ensis and another shrimp (Litopenaeus vannamei).
Journal: Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology - Volume 153, Issue 3, July 2009, Pages 268–274