scholarly journals DISTRIBUTION OF LEUCYL NAPHTHYLAMIDASE AND ALKALINE PHOSPHATASE ON THE VILLI OF THE CHICK DUODENUM

1970 ◽  
Vol 18 (6) ◽  
pp. 416-423 ◽  
Author(s):  
ROBERT D. GREY ◽  
THOMAS S. LECOUNT
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Protein Content ◽  
Age Groups ◽  
Phenyl Phosphate ◽  
Serial Samples

Serial samples from successive levels of the villi and crypts were collected by sectioning a flattened piece of frozen duodenum parallel to the gut wall. Hatched chicks of 1 and 4 weeks of age were studied. Groups of sections were pooled for assay of enzyme activity and protein content. In both age groups, leucyl naphthylamidase was present in the crypts and highest at the bases of the villi while alkaline phosphatase (EC 3.1.3.1) was low or absent in the crypts and highest at the villi tips. Alkaline phosphatase at all levels of the villi hydrolyzed phenyl phosphate faster than β-glycerophosphate; the ratio of activities on these substrates was uniform along the length of the villi, but differed between age groups.

scholarly journals The enzyme activity dynamic relationship with the content of structural polypeptides of enterocyte membranes in cattle fetal

2021 ◽  
Vol 4 (2) ◽  
pp. 3-6
Author(s):  
D. M. Masiuk
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Protein Content ◽  
Apical Membrane ◽  
Basolateral Membrane ◽  
Molecular Weights ◽  
Dynamic Relationship ◽  
Molecular Masses ◽  
Alkaline Activity ◽  
The Relationship

The article performs new data on the relationship between the hydrolytic and transport enzyme activity at different poles of the enterocytes plasmolemma of cow's fetal large intestine with the content of individual fractions of polypeptides. An expressive direct dependence of enzyme activity dynamics on the apical and basolateral membranes of enterocytes containing low molecular weight proteins and an inverse relationship with the concentration of proteins with medium and large molecular weights has been proved. It was found that the alkaline activity of the phosphatase and γ-glutamyltransferase on the apical domain of enterocyte plasmolemma is directly related to the proteins content with molecular masses of 9.6–14.2 kD, 21 kD, 22.5 kD, 26 kD, 33 kD, 35 kD, 170–185 kD, and 205 kD (P ≤ 0.05–0.001). Gamma-glutamyltransferase activity is straightly related to protein quantity with molecular weights of 15.5 kDa and 39 kD (P ≤ 0.05). In contrast, alkaline phosphatase and GGT activity have inverse correlations with the content of polypeptides with molecular masses of 46 kD, 63 kD, and 250 kD in the apical membrane of enterocytes (P ≤ 0.01–0.001). The lactase activity in the cattle enterocytes apical membrane during the test period has significant direct correlations only with the amount of the polypeptide of polypeptides with molecular weights of 31 kD, 39 kD, and 100 kD (P ≤ 0.05–0.01) and inverse relationships containing proteins with molecular masses of 46 kD and 120 kD (P ≤ 0.05). A linear dependence of the different ATPase activity of the apical membrane of red blood cells containing proteins with molecular weights of 9.6–14.2 kD, 15.5 kD, 21 kD, 22.5 kD, 33 kD, 35 kD, 39 kD, and 205 kD (P ≤ 0.05–0.001) was observed. Alkaline phosphatase activity in the apical membrane of enterocytes is only directly related to the number of proteins with molecular weights of 17 kD and 24 kD (P ≤ 0.001) in this domain. It inversely depends on the content of proteins with molecular masses of 9.6–14.2 kD and 52 kD (P ≤ 0.001). G-glutamyltransferase activity is inversely related to protein content with molecular weights of 43 kD, 52 kD, 66 kD, 87 kD, and 100 kD and 155 kD (P ≤ 0.001). The Ca2+, Mg2+-ATPase of the basolateral membrane activity of enterocytes is directly related to the protein amount with molecular weights of 26 kD (P ≤ 0.01), Mg2+-ATPase and Mg2+-ATPase with protein content with the molecular value of 100 kD (P ≤ 0.05).

scholarly journals Inhibition studies of alkaline phosphatase in hard tissue-forming cells.

1975 ◽  
Vol 23 (5) ◽  
pp. 342-347 ◽  
Author(s):  
A Linde ◽  
B C Magnusson
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Adenosine Triphosphatase ◽  
Ruthenium Red ◽  
Inorganic Pyrophosphatase ◽  
Alkaline Ph ◽  
Hard Tissue ◽  
Assay Condition ◽  
Phosphatase Inhibitors ◽  
Inhibition Studies

The effects of the alkaline phosphatase inhibitors levamisole and R 8231 on p-nitro-phenylphosphatase, inorganic pyrophosphatase and adenosine triphosphatase (ATPase) activities in dentingenically active odontoblasts were studied. The p-nitrophenylphosphatase and inorganic pyrophosphatase activities were inhibited, while 40% of the ATP-splitting enzyme activity remained under the assay condition used. This finding, togeather with earlier studies, indicates that at least two different phosphatase are active at alkaline pH in hard tissue-forming cells; on nonspecific alkaline phosphatase and one specific ATPase. The ATPase activity is uninfluenced by ouabain and ruthenium red and is activated by Ca-2+ ions.

scholarly journals Increase in alkaline phosphatase activity in calvaria cells cultured with diphosphonates

1979 ◽  
Vol 183 (1) ◽  
pp. 73-81 ◽  
Author(s):  
R Felix ◽  
H Fleisch
Keyword(s):  
Alkaline Phosphatase ◽  
Protein Synthesis ◽  
Enzyme Activity ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Heat Inactivation ◽  
High Concentration ◽  
Control Value ◽  
Km Value ◽  
Inhibitor Of Protein Synthesis

1. Dichloromethanediphosphonate and to a lesser degree 1-hydroxyethane-1,1-diphosphonate, two compounds characterized by a P-C-P bond, increased the alkaline phosphatase activity of cultured rat calvaria cells up to 30 times in a dose-dependent fashion. 2. Both diphosphonates also slightly inhibited the protein synthesis in these cells. 3. Thymidine, an inhibitor of cell division, did not inhibit the induction of the enzyme, indicating that the increase in enzyme activity was not due to the formation of a specific population of cells with high alkaline phosphatase activity. 4. The effect on alkaline phosphatase was suppressed by the addition of cycloheximide, an inhibitor of protein synthesis. 5. After subculturing the stimulated cells in medium without diphosphonates, the enzyme activity fell almost to the control value. 6. Bovine parathyrin diminished the enzyme activity of the control cells and the cells treated with dichloromethanediphosphonate; however, at high concentration the effect of parathyrin was greater on the diphosphonate-treated cells than on the control cells. 7. The electrophoretic behaviour, heat inactivation, inhibition by bromotetramisole or by phenylalanine, and the Km value of the induced enzyme were identical with that of the control enzyme.

SIGNIFICANCE OF TRANSAMINASE ACTIVITY OF SERUM

PEDIATRICS ◽  
1959 ◽  
Vol 24 (3) ◽  
pp. 360-361
Author(s):  
SAMUEL P. BESSMAN
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Transaminase Activity ◽  
Specific Approach ◽  
Normal Tissues ◽  
The Past ◽  
Glycolytic Activity ◽  
Enzyme Characteristic ◽  
Phosphatase Alkaline

THE MEASUREMENT of enzyme activity of serum as an indicator of disease has a long history in medicine. In the past, it has been the aim of the designers of these methods to make them as specific as possible for assay of an enzyme characteristic of a particular system or group of similar organs. Examples of these venerable tests are those for amylase, acid phosphatase, alkaline phosphatase and choline esterase in the serum. Warburg made the first departure from this specificity by demonstrating that the activity of triosephosphate dehydrogenase in the serum of animals with cancer was much greater than that of controls. This test was partially specific, for as Warburg had earlier shown, the glycolytic activity of tumors is much greater than that of normal tissues. The non-specific approach became extreme with the introduction of the measurement of the glutamic-oxalacetic transaminase reaction in the diagnosis of acute coronary disease.

Acid phosphatase, alkaline phosphatase, and nitrate reductase activity of selected ectomycorrhizal fungi

1989 ◽  
Vol 67 (3) ◽  
pp. 750-753 ◽  
Author(s):  
Iwan Ho
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Nitrate Reductase ◽  
Phosphatase Activity ◽  
Ectomycorrhizal Fungi ◽  
Acid Phosphatase Activity ◽  
Nitrate Reductase Activity ◽  
Reductase Activity ◽  
Phosphatase Alkaline

Seventeen isolates, encompassing five genera and eight species of ectomycorrhizal fungi, were compared for acid phosphatase, alkaline phosphatase, and nitrate reductase activity. Isolates within species differed in enzyme activity and isozyme patterns by host specificity and site (as exemplified by the genus Suillus). Host and site may have affected phosphatase enzyme activity. Generally, the Douglas-fir associates, which dominate in mesic sites, have higher acid phosphatase activity than pine associates, which mostly occupy xeric sites; however, pine associates from mesic sites also have higher acid phosphatase activity (e.g., S. tomentosus). In four isolates of Amanita muscaria, the effect of site was also apparent. Two of them, which have significantly higher acid phosphatase activity than the others, were isolated from mesic sites. The isozyme pattern of the genus Suillus appeared to be separated by host groups. Other isolates with only one species also differed more or less by host groups. They shared at least one band within host groups, except for the two isolates of Paxillus involutus from different hosts. The P. involutus S-403 isolated from an orchard showed much higher nitrate reductase activity than all other isolates. No apparent differences in nitrate reductase activity were found between the other isolates.

Extracellular alkaline phosphatase from marine bacteria: purification and properties of extracellular phosphatase from a marine Pseudomonas sp.

1980 ◽  
Vol 26 (7) ◽  
pp. 833-838 ◽  
Author(s):  
Hiromi Kobori ◽  
Nobuo Taga
Keyword(s):  
Molecular Weight ◽  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Marine Bacteria ◽  
Divalent Cations ◽  
Maximal Activity ◽  
Pseudomonas Sp ◽  
Purification And Properties ◽  
Extracellular Alkaline Phosphatase ◽  
Increased Pressure

Extracellular alkaline phosphatase produced by a marine Pseudomonas was purified to electrophoretic homogeneity. The molecular weight of the enzyme was estimated to be 100 000. The enzyme had maximal activity at pH 11.5. The enzyme was completely inhibited by 1 mM EDTA. However, divalent cations reversed the enzyme inhibition and their order of effectiveness on the reaction was Zn2+ > Ca2+ > Mn2+ > Mg2+ > Sr2+ > Co2+. The enzyme activity was affected by the species of anion whose order of effectiveness was demonstrated to follow the lyotrophic series, Cl− > Br− > NO3−> ClO4− > SCN−. The activity of phosphatase was accelerated linearly by increased pressure until up to 1000 atm (1 atm = 101.325 kPa), and the enzyme activity at 1000 atm was 3.2 times higher than that at 1 atm.

scholarly journals Selenium-dependent glutathione peroxidase protein and activity: immunological investigations on cellular and plasma enzymes

Blood ◽  
1986 ◽  
Vol 68 (3) ◽  
pp. 640-645 ◽  
Author(s):  
K Takahashi ◽  
HJ Cohen
Keyword(s):  
Enzyme Activity ◽  
Glutathione Peroxidase ◽  
Protein Content ◽  
Polyclonal Antibodies ◽  
Plasma Enzyme ◽  
Plasma Enzymes ◽  
Erythrocyte Enzyme ◽  
Dependent Protein ◽  
Gshpx Activity ◽  
Almost All

Selenium-deficient humans and animals are known to be deficient in glutathione peroxidase (GSHPx) activity in their cells and plasma. To determine the relationship between enzyme activity and protein content, the enzyme was purified from human erythrocytes, and polyclonal antibodies were made against the purified protein in rabbits. These antibodies were found to be monospecific, noninhibitory, and capable of precipitating the enzymatic activity. All the GSHPx activity in erythrocytes and almost all the activity in neutrophils and platelets was precipitated by these antibodies. None of the plasma enzyme was precipitated by these antibodies, indicating that the plasma enzyme activity was attributable to a different selenium dependent protein moiety. Utilizing a radioimmunoassay, we were able to determine that there was a direct relationship between GSHPx activity and protein content in the erythrocytes of both normal and selenium-deficient individuals, and a similar relationship between control and selenium- deficient rat erythrocytes and liver cells. Thus, the ability to examine GSHPx as a protein resulted in two new observations concerning the selenium-dependent GSHPx. The first is that the plasma enzyme is antigenically distinct from the erythrocyte enzyme, and the second is that in the absence of selenium, there is a concomitant decrease in GSHPx protein.

DYNAMICS OF ENZYME ACTIVITY AND SOME BLOOD ELEMENTS IN SHEEP PARASITOSIS

2021 ◽  
pp. 40-44
Author(s):  
A. N. Dudarchuk
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Gastrointestinal Tract ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Trointestinal Tract ◽  
Blood Elements

The article presents some studies on study of some aspects of pathogenesis in associative parasitosis of gas-trointestinal tract of sheep. As a result of the conducted studies, it was found that during spontaneous invasion of sheep by associations of parasites of gastrointestinal tract, following changes were established: a significant decrease in number of red blood cells by 1,77 times (P<0,001), hemoglobin-by 39,86 % (P<0,001), an increase in alanineaminotransferase and aspartateaminotransferase – by 1,59 times (P<0,01) and 1,42 times (P<0,001), alkaline phosphatase – by 1,32 times (P<0,001).

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