Histidine metabolism in mackerel (Scomber scombrus). Studies on histidine decarboxylase activity and histamine formation during storage of flesh and liver under sterile and non-sterile conditions

2007 ◽  
Vol 14 (2) ◽  
pp. 131-139 ◽  
Author(s):  
JOSÉ FERNÁNDEZ-SALGUERO ◽  
IAN M. MACKIE
Keyword(s):  
Histidine Decarboxylase ◽  
Decarboxylase Activity ◽  
Scomber Scombrus ◽  
Histamine Formation ◽  
Histidine Decarboxylase Activity

Histamine formation in the blood and bone marrow of the guinea pig

1965 ◽  
Vol 208 (1) ◽  
pp. 186-189 ◽  
Author(s):  
Dorothea Aures ◽  
Gösta Winqvist ◽  
Eskil Hansson
Keyword(s):  
Bone Marrow ◽  
Guinea Pigs ◽  
Histidine Decarboxylase ◽  
Fold Increase ◽  
Histamine Content ◽  
Foreign Protein ◽  
Decarboxylase Activity ◽  
Histamine Concentration ◽  
Histamine Formation ◽  
Histidine Decarboxylase Activity

The histamine content and the histidine decarboxylase activity of bone marrow have been studied in guinea pigs treated with foreign protein. In some experiments the effect of 6-methylprednisolone also was observed. Treatment of guinea pigs with foreign protein resulted in a 10-fold increase of both histamine concentration and histidine decarboxylating activity in the blood and bone marrow. Histamine levels and histidine decarboxylating activity were related to the number of basophils. A fairly constant relationship was found between the histamine content and the enzyme activity per basophil. The findings suggest that histamine is formed and to a certain extent also stored in the basophilic leukocytes.

Production of Histidine Decarboxylase and Histamine by Proteus morganii

1981 ◽  
Vol 44 (11) ◽  
pp. 815-820 ◽  
Author(s):  
R. R. EITENMILLER ◽  
J. W. WALLIS ◽  
J. H. ORR ◽  
R. D. PHILLIPS
Keyword(s):  
Ambient Temperature ◽  
Histidine Decarboxylase ◽  
Maximal Activity ◽  
Reaction Rates ◽  
Decarboxylase Activity ◽  
Acid Ph ◽  
Histamine Formation ◽  
Uninoculated Control ◽  
Histidine Decarboxylase Activity

Examination of 22 Proteus morganii strains revealed that each possessed histidine decarboxylase activity. Strain GRMO 6 produced maximal activity (nanomoles of CO2 released/mg cells/h) when grown at ambient temperature (24 C) and at acid pH levels that tended to inhibit growth. Minimal activity was present when the culture was grown at pH 8.5. Histidine decarboxylase activity decreased as the age of the culture increased. Maximal reaction rates occurred at 37 C and pH 6.5. Rapid enzyme and histamine formation occurred in tuna fillets inoculated with P. morganii and stored at 24 and 30 C. Histamine levels reached 520 mg/100 g and 608 mg/100 g at 24 and 30 C, respectively. Little enzyme was produced in the inoculated fillets stored at 15 C and in the uninoculated control fillets.

Mast cells and histamine concentration in muscle and liver of dystrophic mice

1964 ◽  
Vol 206 (2) ◽  
pp. 338-340 ◽  
Author(s):  
Pierre Bois
Keyword(s):  
Mast Cells ◽  
Histidine Decarboxylase ◽  
Binding Capacity ◽  
The Other ◽  
Decarboxylase Activity ◽  
Histamine Concentration ◽  
Other Hand ◽  
Histamine Binding ◽  
Dystrophic Mice ◽  
Histidine Decarboxylase Activity

The distribution of mast cells in muscle and liver of dystrophic mice was studied; histamine and histidine decarboxylase activity was also measured in the same tissues. Mast cells were significantly more numerous in dystrophic muscles. On the other hand, very few cells could be counted in the liver of either control or dystrophic animals. Histamine concentration was higher in muscle and liver of dystrophic mice; no visible increase in histidine decarboxylase activity could be measured by the methods used. It is concluded that histamine-binding capacity is increased in some tissues of dystrophic mice.

Regulation of rat stomach histidine decarboxylase activity by the serum gastrin concentration

1973 ◽  
Vol 3 (3) ◽  
pp. 178-179 ◽  
Author(s):  
R. Håkanson ◽  
G. Liedberg ◽  
J. Oscarson ◽  
J. F. Rehfeld ◽  
F. Stadil
Keyword(s):  
Histidine Decarboxylase ◽  
Serum Gastrin ◽  
Decarboxylase Activity ◽  
Rat Stomach ◽  
Serum Gastrin Concentration ◽  
Histidine Decarboxylase Activity

Elevation of histidine decarboxylase activity in skeletal muscles and stomach in mice by stress and exercise

2000 ◽  
Vol 279 (6) ◽  
pp. R2042-R2047 ◽  
Author(s):  
Kentaro Ayada ◽  
Makoto Watanabe ◽  
Yasuo Endo
Keyword(s):  
Muscle Activity ◽  
Skeletal Muscles ◽  
Histidine Decarboxylase ◽  
Muscle Tension ◽  
The Other ◽  
Decarboxylase Activity ◽  
Gastric Hemorrhage ◽  
Different Types ◽  
Cold Restraint ◽  
Histidine Decarboxylase Activity

The effects of different types of stress (water bathing, cold, restraint, and prolonged walking) on histidine decarboxylase (HDC) activity in masseter, quadriceps femoris, and pectoralis superficial muscles, and in the stomach were examined in mice. All of these stresses elevated gastric HDC activity. Although water bathing, in which muscle activity was slight, was sufficiently stressful to produce gastric hemorrhage and to increase gastric HDC activity, it produced no detectable elevation of HDC activity in any of the muscles examined. The other stresses all elevated HDC activity in all three muscles. We devised two methods of restraint, one accompanied by mastication and the other not. The former elevated HDC activity in the masseter muscle, but the latter did not. These results suggest that 1) HDC activity in the stomach is an index of responses to stress, 2) the elevation of HDC activity in skeletal muscles during stress is induced partly or wholly by muscle activity and/or muscle tension, and 3) stress itself does not always induce an elevation of HDC activity in skeletal muscles.

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