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At least 1,045 records · Page 58Linked to original sources
PubMed1983

Alkaline phosphatase immuno-enzymatic technique in the diagnosis of pemphigus vulgaris.

Alkaline phosphatase was used in an immuno-enzymatic procedure to detect tissue-bound and circulating antibodies in pemphigus vulgaris. Pemphigus antibodies were revealed by a direct method using alkaline phosphatase conjugated goat anti-human IgG. Cryostat sections were incubated with the specific antiserum, and alkaline phosphatase activity was then revealed histochemically either by Gomori's technique or by the azo dye method. The sections were examined by light microscopy and intercellular staining was demonstrated in the epidermis. The indirect method, in which the patient's serum was incubated with sections of normal skin, gave similar results. Using parallel sections, an immunofluorescent technique was used to demonstrate tissue-bound and circulating antibodies. The alkaline phosphatase method appeared to be slightly less sensitive than the immunofluorescent method.

Alkaline Phosphatase↗
PubMed1979

Occurrence of immunoglobulin G-alkaline phosphatase complexes in human serum.

We studied three patients in whom all or part of their serum alkaline phosphatase circulated as a complex with immunoglobulin G (IgG). Serum alkaline phosphatase isozymes were visualized by their electrophoretic (in agar, agarose, and starch gel and on cellulose acetate), gel filtration, and electroimmunodiffusion behaviour. The alkaline phosphatase-IgG complex was of the liver type (two cases) and bone type (one case). The reaction pattern of alkaline phosphatase with different human tissues and with sera of heterologous origin suggests that the complex is of the antigen-antibody type. A direct genetic mechanism seems unlikely since in one patient the IgG-alkaline phosphatase complex was not present in previous serum samples. The presence of this complex has no apparent correlation with the observed abnormalities. Alkaline phosphatase linked to immunoglobulin G must be considered in the interpretation of increased serum alkaline phosphatase.

Aged↗
PubMedDate not supplied

Thermally stabilized immunoconjugates: conjugation of antibodies to alkaline phosphatase stabilized with polymeric cross-linkers.

A method of conjugating poly(glutamic acid) poly(phosphorothioate)-cross-linked alkaline phosphatase to maleimide-derivatized immunoglobulin is described. Intramolecular autocatalyzed cross-linking of alkaline phosphatase at 2:1 to 4:1 polymer:enzyme ratios introduced 32-68 thiolates on the surface of the enzyme. Depending on the stoichiometry of polymer to enzyme, the cross-linked alkaline phosphatase retained 75-90% of its native catalytic activity. The cross-linked thiolate-functionalized alkaline phosphatase was conjugated to maleimide-derivatized immunoglobulin. Compared to a control prepared using non-cross-linked alkaline phosphatase, these conjugates were smaller in size and more stable to heat. The enzymatic activity of the cross-linked conjugates after incubation at 45 degrees C and pH 7.5 for 25 days was 35% higher than those of the highest-activity control conjugates. The conjugation process could be controlled by varying the stoichiometries of poly(glutamic acid) poly(phosphorothioate), alkaline phosphatase, and immunoglobulin.

Alkaline Phosphatase↗
PubMed1981

Origin of urinary alkaline phosphatase excreted by cadmium-treatment of rabbits.

In order to ascertain the origin of increased alkaline phosphatase in the urine of rabbits with injured proximal tubules, we studied the phosphatase by an isoenzyme examination, an inhibition test and an inactivation test. Male rabbits were daily injected subcutaneously with cadmium chloride at a dose of 1.5 mg Cd/kg/day. After treatment for three weeks, total activity of alkaline phosphatase and its isoenzyme patterns on agar-gel and disc-gel electrophoresis were examined in the liver, kidney cortex, plasma and urine, and compared with those of the control rabbits. Alkaline phosphatase activity in the urine of the cadmium treated rabbit was about eleven times higher than that of the control (p = less than 0.005), while enzyme activity of plasma showed almost no difference between the two groups. The isoenzyme patterns of alkaline phosphatase in both agar-gel and disc-gel electrophoresis showed that the main band of the isoenzymes of alkaline phosphatase obtained from urine of control rabbits migrated faster than that from plasma, liver, or kidney, while the main isoenzyme from urine of the cadmium group was consistent with the rapid migrating isoenzyme obtained from the kidney. Furthermore, in both groups, alkaline phosphatase activity in plasma was inactivated by the treatments of heat and urea, and inhibited by L-homoarginine, while the enzymes of the kidney and urine were not remarkably effected. The findings suggest that the increased urinary excretion of the enzyme after administration of cadmium to rabbits originates from the kidney.

Alkaline Phosphatase↗
PubMed1989

[Granulocyte alkaline phosphatase and myeloperoxidase in patients with ischemic heart disease].

Alkaline phosphatase and myeloperoxidase was examined in patients with chronic ischemic heart disease and myocardial infarction. It was established that patients with myocardial infarction showed high values of alkaline phosphatase while the values of myeloperoxidase were low. Dynamic evaluation of alkaline phosphatase and myeloperoxidase of leucocytes allows to assess the course of myocardial infarction and efficacy of its treatment.

Aged↗
PubMed1979

Release of alkaline phosphatase activity by aqueous-ether treatment of whole cells of Serratia marcescens.

The effect of aqueous-ether treatment according to the method of Ribi et al. (1961) on the release of alkaline phosphatase from cells of two strains of Serratia marcescens was studied. By this method, lipopolysaccharide-protein (endotoxin) complexes associated with alkaline phosphatase activities were released from both strain 08 and strain Bizio. SDS-polyacrylamide gel electrophoresis followed by enzymatic assay showed the presence of two active components in each strain. Fractions released from strain 08 contained alkaline phosphatase A (140,000 dalton) and alkaline phosphatase B (110,000) daltons) while those from strain Bizio contained alkaline phosphatase A' (190,000 daltons) and alkaline phosphatase B (110,000 daltons). Although it is known that saline plays a role in the release of alkaline phosphatase activities from cell envelope of Gram-negative bacteria the presence of saline in the extracting medium affects only slightly the chemical composition and not at all on the enzymatic nature of the released components. By comparing the enzymatic profiles of the materials released by other techniques, such as polymyxin B treatment and osmotic shock, it appears that alkaline phosphatase activities released by aqueous-ether treatment of whole cells of S. marcescens originate from the periplasmic space.

Alkaline Phosphatase↗
PubMed1993

Individual and combined effects of intact PTH, amino-terminal, and a series of truncated carboxyl-terminal PTH fragments on alkaline phosphatase activity in dexamethasone-treated rat osteoblastic osteosarcoma cells, ROS 17/2.8.

The individual and combined effects of intact PTH, amino-terminal, and a series of truncated carboxyl-terminal PTH fragments on alkaline phosphatase activity were examined in dexamethasone-treated rat osteoblastic osteosarcoma cells ROS 17/2.8. Dexamethasone-induced alkaline phosphatase activity was inhibited not only by hPTH(1-84) and amino-terminal PTH fragment hPTH(1-34), but also by carboxyl-terminal PTH fragment hPTH(69-84) in a dose-related fashion. At 10(-7) mol/l, hPTH(1-84) completely abolished dexamethasone-induced alkaline phosphatase activity, while hPTH(1-34) and hPTH(69-84) reduced alkaline phosphatase activity to 0.16 +/- 0.02 and 0.80 +/- 0.03 fold, respectively, of the control value obtained in the absence of PTH peptides. The combination of hPTH(1-34) and hPTH(69-84) resulted in reduction of alkaline phosphatase activity to the level obtained by hPTH(1-84). The shorter carboxyl-terminal PTH fragment hPTH(71-84) did not affect alkaline phosphatase activity or modulate the action of hPTH(1-34). The longer carboxyl-terminal PTH fragment hPTH(53-84) stimulated alkaline phosphatase activity up to 1.23 +/- 0.03 fold and partially blunted the inhibitory effect of hPTH(1-34) on alkaline phosphatase activity. These findings suggest that carboxyl-terminal PTH fragments could exert diverse effects on the target cells, depending on the length of deletion of amino-terminal amino acids of PTH molecule, and interact with amino-terminal PTH fragment. The two amino-terminal amino acids of hPTH(69-84) and the 53-68 portion of hPTH(53-84) might be responsible for the respective inhibitory and stimulatory effects of the peptides on alkaline phosphatase activity.

Alkaline Phosphatase↗
PubMed1986

Changes of acid and alkaline phosphatase activities in the developing mouse brain.

Acid and alkaline phosphatase activities in the mouse cerebrum, brainstem and cerebellum increased during the late fetal and perinatal period and reached a maximum on postnatal day 28 (P28). Myelination was most extensive on P28-P45 in the brainstem and in the cerebellum, and phosphatidic acid phosphatase activity concomitantly decreased to a low level after birth. The changes in acid and alkaline phosphatase activities correlate more with the extent of myelination than with the overall brain tissue growth.

Acid Phosphatase↗
PubMed1983

Influence of taurocholate on hepatic clearance and biliary excretion of asialo intestinal alkaline phosphatase in the rat in vivo and in isolated perfused rat liver.

We have used canine intestinal alkaline phosphatase, an asialoglycoprotein, as a tool to study the effect of taurocholate on hepatic asialoglycoprotein transport. After bolus injections of 20 U of alkaline phosphatase into anesthetized rats in vivo and isolated perfused rat livers, a biexponential disappearance pattern was observed; 6.2% of the dose and 0.8% of the dose was excreted in bile, respectively. Taurocholate infusion in vivo and in isolated perfused livers resulted in a virtually complete abolition of the plasma disappearance of alkaline phosphatase in the second slow phase of the curve, whereas the primary disappearance rate was not affected. Wash out experiments showed release of exogenous alkaline phosphatase from the liver, which was strongly increased by taurocholate. Liver perfusion experiments with two subsequent doses of alkaline phosphatase indicated that the taurocholate effect was completely reversible. It is concluded that taurocholate enhances exocytosis of interiorized alkaline phosphatase from liver into plasma. The taurocholate effect on hepatic exocytosis of the asialoglycoprotein may also occur when bile salt concentrations in the systemic or portal circulation, or both, are elevated due to certain liver diseases and postprandial bile salt absorption.

Alkaline Phosphatase↗
PubMed1977

Hepatic alkaline phosphatase isoenzymes: isolation, characterization and differential alteration.

Although it is generally believed that hepatic alkaline phosphatase is localized to liver plasma membranes, 63% is present in the cytosol fraction after ultracentrifugation of rat liver homogenates. Divalent cation requirements, heat inactivation, pH optima, Km and chemical inhibition characteristics of partially purified alkaline phosphatase enzymes prepared from membrane and cytosol fractions suggested different structural forms. Furthermore, bile duct obstruction and ethinyl estradiol administration preferentially increased membrane-bound alkaline phosphatase activity, while cytosol activity was unaltered. In contrast, phenobarbital treatment decreased membrane-bound alkaline phosphatase and increased cytosol activity. These studies support the presence of two forms of hepatic alkaline phosphatase in rat liver which are regulated by different control mechanisms.

Alkaline Phosphatase↗