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, Volume 10, Issue 1–2, pp 92–93 | Cite as

Purification and immunochemical analysis of histidine decarboxylase from murine mastocytoma

  • Lena Hammar
  • Stellan Hjertén
Histamine and Kinins Histamine Metabolism

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.

Keywords

Histidine Major Protein Histidine Decarboxylase Immunochemical Analysis Reasonable Stability 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

References

  1. [1]
    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.Google Scholar
  2. [2]
    L. Hammar andS. Hjertén,Mammalian Histidine Decarboxylase; Changes in Molecular Properties Induced by Oxidation and Reduction, Agents and Actions, (this issue).Google Scholar

Copyright information

© Birkhäuser Verlag 1980

Authors and Affiliations

  • Lena Hammar
    • 1
  • Stellan Hjertén
    • 1
  1. 1.Institute of Biochemistry, Biomedical CenterUniversity of UppsalaUppsalaSweden

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