Gastric histidine decarboxylase

Autor: Phyllis E. Powell, M. Ashwini Kumar
Rok vydání: 1968
Předmět:
Zdroj: Analytical Biochemistry. 22:485-492
ISSN: 0003-2697
Popis: A simple method is described for determining histidine decarboxylase activity. It depends on the measurement of 14 CO 2 liberated from tracer carboxyl- 14 C- l -histidine. The method is sensitive enough to permit measurements in small samples of gastric mucosa of individual rats. It is specific in that dopa decarboxylase does not interfere. The enzyme has constant K m values of 5 × 10 −4 M between pH 6 and 8, while the maximum reaction velocity has an optimum near pH 7. The enzyme content is high in the ruminal and main gastric and low in pyloric antral mucosa. Food intake enhances enzyme activity.
Databáze: OpenAIRE