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Comparaison immunochimique de quelques phosphagene kinases de muscle

1970; Pergamon Press; Volume: 32; Issue: 3 Linguagem: Inglês

10.1016/0010-406x(70)90457-3

1879-3029

B. Viala, Y Robin, Nguyen‐Van Thoai,

Venomous Animal Envenomation and Studies

1. The immunochemocal properties of a number of phosphagen kinases from vertebrate and invertebrate muscle have been studied. 2. By gel diffusion methods, cross-reactions were occasionally noticed between similar enzymes of different species, demonstrating immunological analogies within some zoological groups. 3. For creatine kinase, these results contrast with the absence of cross-reactions reported between the two pure isozymic forms (muscle and brain type) of one species. 4. No cross-reactions occur between arginine kinase and creatine kinase, nor between these enzymes and the other phosphagen kinases. 5. On the other hand, cross-reactions were detected between lombricine, opheline and taurocyamine kinases, the three enzymes specific for oligochaetous and polychaetous annelids. 6. All phosphagen kinases studied were inhibited by their specific antiserum, but no cross-inhibition occurred between heterologous antigens. 7. The results suggest that the inhibition involves steric hindrance and that the antibodies are formed against other sites than the active sites. 8. It is suggested that mild denaturation of the phosphagen kinases could create similar antigenic determinants on their molecules, as has been found for lactic dehydrogenases. 9. From a phylogenetic point of view, the immunochemical study of native phosphagen kinases show the partial conservation of the protein structure through evolution. 10. The analogies so noticed seem to depend on the animal origin of the protein rather than on its specificity toward the natural guanidine substrate.