Acid phosphatase activity in the chick ovary during embryonic development

Acid phosphatase activity was studied in the left and right ovaries of the chick during embryonic development. The cytochemical study indicated that local enzymatic activity is localized mainly in germ and somatic cells. From the results obtained in the study on the specific activity of this acid hydrolase, it can be inferred that the higher concentration of this enzyme in the right ovary would be determined by a decrease of total proteins in the total homogenate and in the cellular fractions of this organ. Besides, a decrease in the enzymatic activity of this ovary is not observed, but it occurs in the left ovary. This finding would indicate a lack of enzymatic segregation that could be related to the phenomenon of ovarian atrophy. Finally, the electrophoretic study indicated that it would apparently exist only one molecular form of the enzyme. Our results support the hypothesis that acid phosphatase would be involved in the atrophic processes of the right ovary during embryonary differentiation.     

Alkaline phosphatase activity of duodenal enterocytes after neonatal administration of monosodium glutamate to rats

In the present work neonatal male and female Wistar rats were treated intraperitoneally with monosodium glutamate (MSG 2 mg/kg b.w.) or saline (controls) daily for 4 day after birth. At the age of 30 and 80 days, the alkaline phosphatase activity (AP) in the brush border of individual enterocytes, the body fat content and Lee's index of obesity were analyzed. Microdensitometrical quantification of AP was significantly increased on day 30 in males (P<0.01) and on day 80 in MSG-treated male and female rats (P<0.001) as compared to the controls. MSG administration also increased the body fat weight and the obesity index significantly (P<0.001) in 80-day-old animals, but was without any significant effect on their food intake. Our results showed that a) neonatal MSG-treatment may significantly change the intestinal function and b) the investigation of the intestinal enzyme activities may be important in further studies on MSG-induced and other forms of obesity.     

Alkaline phosphatase activity of the mouse

Plasma alkaline phosphatase (PAP) activity of young adult CD mice is low (e.g. 1/10th of that of rat) and is lower in males than in females. The variability of PAP was assessed in groups of mice kept under different husbandry conditions (e.g. caging, diet, SPF). PAP activities of fed and fasted mice are similar. After comparing their acrylamide electrophoresis and the action of several inhibitors upon the PAP and the alkaline phosphatase of various organ extracts, it is suggested that the two isoenzymes of PAP (indicated by heat inhibition) probably arise from bone and liver.     

Alkaline phosphatase activity of rumen bacteria

Of the 54 strains of rumen bacteria examined for alkaline phosphatase (APase) production, 9 of 33 gram-negative strains and none of 21 gram-positive strains produced the enzyme. The APase of the cells of the three strains of Bacteroides ruminicola that produced significant amounts of the enzyme was located in the periplasmic area of the cell envelope, whereas the enzyme was located in the strains of Selenomonas ruminantium and Succinivibrio dextrinosolvens was associated with the outer membrane. The localization of APase production in the cells of natural populations of rumen bacteria from hay-fed sheep was accomplished by reaction product deposition, and both the proportion of APase-producing bacteria and the location of the enzyme in the cell envelope of the producing cells could be determined. We suggest that this procedure is useful in detecting shifts in the bacterial population and the release of cell-bound APase that accompany feedlot bloat and other sequelae of dietary manipulation in ruminants.     

Alkaline phosphatase and maltase activity in the embryonic chick intestine in culture. Influence of thyroxine and hydrocortisone.

In strips of duodenum from 14-day chick embryos explanted into defined medium, alkaline phosphatase (ALP) activity accumulated in the tissue at a faster rate than in vivo for about 48 hr, but failed to increase thereafter. The addition of thyroxine (T4) to the medium at 10^?8M or less both enhanced the early accumulation and elicited a very large increase in ALP activity comparable to that normally occurring during the last 2 days in ovo. Activity with phenylphosphate (PhP) was more strongly affected than that with β-glycerophosphate (βGP), so that the high $\text{PhP}\text{β}\text{GP}$ ratio attained in vivo at 18 days was reached after 24 hr in T4-supplemented medium. Hydrocortisone (HC) evoked APL activity only slightly above that in unsupplemented medium and only during the first 48 hr in culture, but it precociously elevated $\text{PhP}\text{β}\text{GP}$ ratio to the normal maximum. In the presence of T4 or HC, maltase activity rose in explanted strips at the same rate as in the intact duodenum, but it lagged in unsupplemented medium. Assay of the medium revealed, however, that under all conditions of culture a large amount of both maltase and ALP activity had been released from the tissue. This effect was especially pronounced in the presence of T4, so that explants and medium together accumulated ALP and maltase equivalent to the high peaks of activity found in the intact duodenum at hatching. With 10^?8M T4, ALP activity began to rise above that of control explants after 8 hr, with accumulation in the medium beginning about 4 hr later. Combining 2 × 10^?6M HC with a range of T4 concentrations produced greater than additive effects, particularly with ALP, but did not lead to enhanced retention of either enzyme in the tissue strips. Prolactin, pentagastrin, and insulin were without effect alone, but the latter inhibited the effects of both T4 and HC.     

Alkaline phosphatase activity of coral reef benthos

Alkaline Phosphatase (AP-ase) activity was measured for a variety of benthic algae and a community of reef organisms. Algae with epiphytic bacteria showed a higher AP-ase activity than algae without bacteria (11.6 mol P g^-1 h^-1 vs. 1.9mol P g^-1h^-1). AP-ase activity associated with the benthos was estimated to be in the range of 10–100 mmol P m^-2d^-1, at least 1000 Cold greater than reported activity in the water column. Enzyme activity of reef benthos at saturated organic phosphate (P) substrate concentrations was sufficiently high that P uptake from organic substrates could be as fast as inorganic P uptake. Organic P compounds may be important in P recycling, but there is no evidence that organic P represents a significant new source of P to coral reefs.     

Alkaline phosphatase activity of rumen bacteria.

Of the 54 strains of rumen bacteria examined for alkaline phosphatase (APase) production, 9 of 33 gram-negative strains and none of 21 gram-positive strains produced the enzyme. The APase of the cells of the three strains of Bacteroides ruminicola that produced significant amounts of the enzyme was located in the periplasmic area of the cell envelope, whereas the enzyme was located in the strains of Selenomonas ruminantium and Succinivibrio dextrinosolvens was associated with the outer membrane. The localization of APase production in the cells of natural populations of rumen bacteria from hay-fed sheep was accomplished by reaction product deposition, and both the proportion of APase-producing bacteria and the location of the enzyme in the cell envelope of the producing cells could be determined. We suggest that this procedure is useful in detecting shifts in the bacterial population and the release of cell-bound APase that accompany feedlot bloat and other sequelae of dietary manipulation in ruminants.