Histidine decarboxylase (EC 4.1.1.22) prepared from a murine mastocytoma is activated up to six-fold when the concentration of phosphate in the assay medium is increased from 1 mM to 150 mM. Chloride and sulfate, on the other hand, are inhibitory and appear to interfere with the binding of pyridoxal
A microassay for mammalian histidine decarboxylase
β Scribed by David G. Ritchie; David A. Levy
- Publisher
- Elsevier Science
- Year
- 1975
- Tongue
- English
- Weight
- 690 KB
- Volume
- 66
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
β¦ Synopsis
This report describes a microassay procedure for mammalian histidine decarboxylase (HDC) based on the measurement of ['YZ]O, formed from L-[l-Wlhistidine.
This assay is particularly useful for quick measurement of HDC activity both in microgram quantities of cell or tissue extract and in tissues that contain significant levels of endogenous histamine.
Using this assay, we have shown that the pH optimum, K, and thermolability of HDC are similar for extracts prepared both from normal rat peritoneal mast cells and from the Furth mouse mastocytoma. HDC activity could be detected in homogenates prepared from IO5 rat mast cells, and it was expressed on a per cell basis. Mast cell HDC activity varied with the strain of rat from which the cells were obtained and with the season when they were assayed.
' In partial fulfillment of the requirements of Johns Hopkins University for the degree of Doctor of Philosophy.
π SIMILAR VOLUMES
Histamine is a multifunctional biogenic amine with relevant roles in intercellular communication, inflammatory processes and highly prevalent pathologies. Histamine biosynthesis depends on a single decarboxylation step, carried out by a PLP-dependent histidine decarboxylase activity (EC 4.1.1.22), a