ISSN:
1365-3083
Quelle:
Blackwell Publishing Journal Backfiles 1879-2005
Thema:
Medizin
Notizen:
Alkaline phosphatase (APase) has been shown to have a membrane-bound localization in the murine fetal thymus, murine thymic lymphoma and in areas of lymphoproliferation of the adult spleen. A detailed biochemical comparison of the lymphoma APase with the fetal thymus, placenta, and spleen APases was performed. The parameters investigated were pH optimum, activation, inhibition, heat inactivation and substrate ratio with the substrate α-naphthyl phosphate. All four murine APase activities have a pH optimum of 10 and were activated by magnesium and nucleophilic buffers to the same extent. The APase activities tested were all inhibited by ethylenediamine tetraacetic acid, L-phenylalanine and L-homoarginine at the same levels, approximately 97%, 8% and 81%, respectively. Substrate ratios indicate that all four APases hydrolyzed both p-nitrophenyl phosphate and α-naphthyl phosphate at the same rate. These data lead one to conclude that the APase of murine thymic lymphoma may represent a cell membrane carcinofetal enzyme.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1111/j.1365-3083.1978.tb03969.x
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