Microheterogeneity of Kasahara isozyme

Clinica Chimica Acta; International Journal of Clinical Chemistry
T HadaJ Sato

Abstract

The microheterogeneity of Kasahara isozyme was investigated by affinity electrophoresis with Con A as the affinity ligand in combination with polyacrylamide gradient gel electrophoresis. On two-dimensional Con A-containing agarose gel electrophoresis, the Kasahara isozyme was separated into three molecular species. Kasahara isozyme electrophoresed as two distinct bands with enzyme activity on polyacrylamide gradient gel, but liver, intestinal or placental alkaline phosphatase showed only one distinct spot or band on both electrophoreses. One of the three molecular species of Kasahara isozyme separated by Con A-containing agarose gel electrophoresis was extracted from the gel and applied to the polyacrylamide gradient gel electrophoresis again, resulting in the same electrophoretic pattern as that of the original Kasahara isozyme. These findings indicated that the Kasahara isozyme consists of at least four molecular species. The same analysis was conducted with alkaline phosphatase of the HuH-6 cl-5 cell line, which has been reported to release an alkaline phosphatase closely resembling the Kasahara isozyme, and the results were compared with those obtained with the Kasahara isozyme.

References

Aug 22, 1975·Annals of the New York Academy of Sciences·K HigashinoY Yamamura
Jul 1, 1975·Annals of Internal Medicine·K HigashinoT Hada
Oct 16, 1978·Clinica Chimica Acta; International Journal of Clinical Chemistry·T HadaY Yamamura

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