High impact information on C14177

• The recombinant protein was purified by affinity chromatography and showed high capacity for phosphorylation of lombricine [1].
• Cloning and expression of a lombricine kinase from an echiuroid worm: insights into structural correlates of substrate specificity [1].
• One of the two cDNA-derived amino acid sequences of TKs shows a high amino acid identity to lombricine kinase, another phosphagen kinase unique to annelids, and appears to be a cytoplasmic isoform [2].
• This sequence is very similar to that of homologous ATP:guanidine phosphotransferases previously studied, arginine kinase from Homarus vulgaris muscle, creatine kinase from ox brain and ox muscle, and from rabbit muscle, and lombricine kinase from Lubricus terrestris [3].

Biological context of C14177

• This is the first reported lombricine kinase amino acid sequence [4].

Associations of C14177 with other chemical compounds

• Evolution of phosphagen kinase. VI. Isolation, characterization and cDNA-derived amino acid sequence of lombricine kinase from the earthworm Eisenia foetida, and identification of a possible candidate for the guanidine substrate recognition site [4].

Analytical, diagnostic and therapeutic context of C14177

• In Experiment 1, daily subcutaneous injections of lombricine (0.3 mg/0.05 ml olive oil) inhibited markedly the growth of tumours associated with the retardation of the growth of preneoplastic mammary hyperplastic alveolar nodules [5].

References