Adenosine 5'-triphosphate-arginine Phosphotransferase from Lobster Muscle: Purification and Properties.
نویسندگان
چکیده
1. A simple chromatographic method is described for the purification of arginine kinase from lobster (Homarus vulgaris) muscle. 2. Some physical properties and the effects on enzyme activity of ionic strength, pH, buffer salts, metal ions and substrates are reported. 3. The kinetic parameters, evaluated by variation of the concentration of one of the substrates, are dependent on the concentration of the other substrate. 4. The properties of the enzyme are discussed in relation to previous findings about phosphagen phosphotransferases.
منابع مشابه
Cloning and sequence analysis of the cDNA for arginine kinase of lobster muscle.
Arginine kinase belongs to an evolutionary conserved family of ATP:guanidino phosphotransferases, whose members play an important role in energy metabolism. In this work, a lambda gt11 lobster muscle library was constructed and screened by using both polyclonal antibodies and two synthetic oligonucleotides. The complete amino acid sequence of arginine kinase (ATP:L-arginine N-phosphotransferase...
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عنوان ژورنال:
- The Biochemical journal
دوره 99 1 شماره
صفحات -
تاریخ انتشار 1965