Abstract
Application of a new scheme of purification for histidine decarboxylase (E.C. 4.1.1.22) leads to a highly purified enzyme (5000 nmol/mg·h, i.p. 5.0, M.W.: 110 kD) with reasonable stability (rest activity 80% after 3 weeks at 6–8°C). A major protein contaminant seen on electrofocusing (i.p. 4.6) shows immunological identity with the enzyme-containing protein (i.p. 5.0) and might be involved in the aggregation of the enzyme.
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References
D. Aures andR. Håkansson,Histidine Decarboxylase (Mammalian), in:Methods in Enzymology, Vol. XVII, part B (Eds. H. Tabor and C. Tabor: Academic Press, New York and London, 1971), pp. 667–677.
L. Hammar andS. Hjertén,Mammalian Histidine Decarboxylase; Changes in Molecular Properties Induced by Oxidation and Reduction, Agents and Actions, (this issue).
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Hammar, L., Hjertén, S. Purification and immunochemical analysis of histidine decarboxylase from murine mastocytoma. Agents and Actions 10, 92–93 (1980). https://doi.org/10.1007/BF02024184
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DOI: https://doi.org/10.1007/BF02024184