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PubMed1990

Assessment of bone turnover in the dry period of dairy cows by measurement of plasma bone GLA protein, total plasma alkaline phosphatase activity and urinary hydroxyproline.

Plasma osteocalcin, or plasma bone GLA protein (BGP), total plasma alkaline phosphatase activity and urinary hydroxyproline excretion of twenty-four pregnant dairy cows (thirteen in their first or second pregnancy, i.e. low parity, and eleven in their third or more pregnancies, i.e. high parity) were measured from 7 weeks before parturition until 1 week after parturition. Seven weeks before parturition the cows' ration was changed to one containing either 0.22% magnesium (low magnesium, LMg) or 0.82% magnesium (high magnesium, HMg) in the dry matter, and the potassium content of both rations was increased to approximately 4.1% in the dry matter to reduce the absorption of magnesium. Plasma BGP levels decreased significantly (P less than 0.01) as parturition approached while total plasma alkaline phosphatase activity and urinary hydroxyproline excretion did not. Magnesium supply and parity had no significant effect on this decrease. The overall plasma concentration of BGP, total plasma alkaline phosphatase activity and the urinary hydroxyproline/creatinine ratio in the prepartum period were affected by parity (P less than 0.05) with higher values in the lower parity cows. A significant positive correlation (r = 0.58, P less than 0.01) was found in all cows between plasma BGP level at parturition and the percentage of the bone surface covered with osteoblasts; however, plasma BGP was not correlated either with other histomorphometric variables or with total alkaline phosphatase activity during this time.

Alkaline Phosphatase↗
PubMed1990

Heat-stable alkaline phosphatase as a marker for human and monkey type-I pneumocytes.

The expression of the heat-stable isoenzyme of alkaline phosphatase in the human and monkey (Macaca mulatta, M. fascicularis) lung was investigated at the light- and electron-microscopic level, using cytochemical techniques and immunocytochemical procedures based on monoclonal and polyclonal antibodies against human term-placental alkaline phosphatase. Both in man and monkey, the enzyme was present in type-I pneumocytes. In the monkey, the enzyme was found in all type-I cells. In man, strong staining was observed only in some type-I cells and in certain cuboidal respiratory bronchiolar cells. Staining was localized on the apical and basal plasma membrane, in apical and basal caveolae, and in the underlying basement membrane. The level of heat-stable alkaline phosphatase expression in the human lung was 10-fold lower than in the monkeys studied. In human fetal lung, the onset of heat-stable alkaline phosphatase expression was associated with the development of the alveolar epithelium from 17-20 weeks gestation onward. It is concluded that: (1) heat-stable alkaline phosphatase is a specific constituent of type-I pneumocytes in man and monkeys; and (2) its subcellular localization may explain its rapid appearance in the circulation under certain conditions.

Alkaline Phosphatase↗
PubMed1981

Screening for liver metastases from colorectal cancer with carcinoembryonic antigen and alkaline phosphatase.

A sensitive and economic method of screening for liver metastases in patients with colorectal cancer was developed using serum alkaline phosphatase and carcinoembryonic antigen. The upper limit of normal for alkaline phosphatase and carcinoembryonic antigen did not represent the optimal levels for use in predicting liver metastases. However, with alkaline phosphatase greater than 135 I.U., and/or carcinoembryonic antigen greater than 10 ng/ml, sensitivity was 88%: 23 of 26 patients with liver metastases fulfilled either or both criteria. The false-positive rate was 12%. Liver scanning, alone, demonstrated metastases in only 69% of 35 patients with liver metastases. The combination of alkaline phosphatase and carcinoembryonic antigen can be used economically to screen for liver metastases, and to determine which patients should undergo a liver scan.

Alkaline Phosphatase↗
PubMed1988

Wheat-germ agglutinin method for measuring bone and liver isoenzymes of alkaline phosphatase assessed in postmenopausal osteoporosis.

In the method of Rosalki and Foo (Clin Chem 1984;30:1182-6) bone and liver isoenzymes of alkaline phosphatase (EC 3.1.3.1) are quantified by using wheat-germ agglutinin (WGA). I suggest standardizing the procedure by using a WGA concentration that precipitates half of the alkaline phosphatase activity of serum pooled from an equal number of healthy women and men. By applying knowledge of the precipitation pattern in serum samples containing predominantly or exclusively bone or liver sources of alkaline phosphatase, I obtained results for the isoenzymes in healthy subjects that agreed with those by the heat-inactivation methods, as reported earlier in the literature. I then assessed the utility of the standardized procedure in a clinical study of prevention of postmenopausal bone loss. In patients receiving hormone replacement therapy, which is known to decrease bone turnover, the decrease in total alkaline phosphatase activity in serum was entirely ascribable to decreases in the bone isoenzyme activity, probably reflecting reduced bone formation, whereas the activity concentration of liver alkaline phosphatase remained unchanged.

Adult↗
PubMed1982

Effect of sodium butyrate on alkaline phosphatase in HRT-18, a human rectal cancer cell line.

Treatment of the human rectal cancer cell line HRT-18 with sodium butyrate caused a reversible elevation of alkaline phosphatase activity which was inhibited by cycloheximide and actinomycin D. The alkaline phosphatase in untreated cells was heat stable at neutral pH and inhibited by phenylalanine but not by homoarginine, and 80% of the enzyme activity was precipitated by antibody against human term-placental enzyme. Following butyrate treatment, the enzyme became more sensitive to all the inhibitors tested and more heat stable, compared to the enzyme in control cells. In addition, the butyrate-induced enzyme could be completely precipitated by anti-placental alkaline phosphatase antibody. The electrophoretic pattern of the butyrate-induced enzyme was different from that of control cells. Control HRT-18 cells contained a butyrate-insensitive heat-labile alkaline phosphatase component with an electrophoretic mobility similar to the enzyme from human colon cancer tissues. The alkaline phosphatase from four human colon cancer tissues was of the early placental form, while the enzyme from human normal mucosa was of the intestinal type.

Alkaline Phosphatase↗
PubMed2002

Study of interaction of export initiation domain of Escherichia coli mature alkaline phosphatase with membrane phospholipids during secretion.

The efficiency of secretion of alkaline phosphatase from Escherichia coli depending on the primary structure of its N-terminal region and the content of zwitterionic phospholipid phosphatidylethanolamine and anionic phospholipids in membranes has been studied in this work to establish the peculiarities of interaction of mature protein during its secretion with membrane phospholipids. It has been shown that the effect of phosphatidylethanolamine but not anionic phospholipids on the efficiency of alkaline phosphatase secretion is determined by the primary structure of its N-terminal region. The absence of phosphatidylethanolamine appreciably reduces the efficiency of secretion of wild type alkaline phosphatase and its mutant forms with amino acid substitutions in positions +5+6 and +13+14. In contrast, secretion of the protein withamino acid substitutions in positions +2+3, significantly decreased as a result of such mutation, in the presence of phosphatidylethanolamine, reaches the level of wild type protein secretion in the absence of phosphatidylethanolamine. The results suggest an interaction of the N-terminal region of the mature protein under its translocation across the membrane with phosphatidylethanolamine.

Adenosine Triphosphate↗
PubMed1975

Histochemical study of the activity of acid and alkaline phosphatases and lipase in the gastro-intestinal tract of Cirrhinus mrigala.

The sites of the activity of acid and alkaline phosphatases and lipase have been localized in the gastro-intestinal tract of the fresh water fish, Cirrhinus mrigala. All the three enzymes experimented have been recorded to be active in the mucosal epithelium of all the portions of the alimentary canal. Muscularis and serosa of all the parts of alimentary canal show negative sign for the presence of these enzymes. In the pancreas, both intra-hepatic and extrahepatic, strong activity of these enzymes is dicernible in the acinar cells. Hepatic cells also show intense reaction for these enzymes. In comparison to acid phosphatase, the activity of alkaline phosphatase is more pronounced in all the portions of the alimentary tract. The positive reaction for lipase in the blood and lymph vessels present in the tissues of the alimentary canal signifies the hydrolysis of fats during their transportation.

Acid Phosphatase↗
PubMed1978

Placental enzyme polymorphism among Maharashtrians: alkaline phosphatase and lactate dehydrogenase.

The distribution of placental alkaline phosphatase and lactate dehydrogenase types in 635 placentas from various endogamous groups of Maharashtra have been studied by starch gel electrophoresis. In the case of alkaline phosphatase, 6 common phenotypes and 6 rare phenotypes (F2I1, S1S2, S2S3, I1S2, F1S2, F1I2) are encountered. The highest frequency of Pls1 allele (0.7394) and lowest frequency of Pli1 allele (0.0246) have been found in the Nava-Budha. 6 cases of Cal-1 and 5 cases of Cal-2 types of LDH variants have been observed in the total samples, and Muslims possess the highest frequency of Cal-1 types (3.64%). Population groups are compared with respect to Pl alleles.

Alkaline Phosphatase↗
PubMed1976

Replacement of metal in metalloenzymes. A lead-alkaline phosphatase.

Lead ions can interact with calf intestine alkaline phosphatase. Experiments using 203Pb-labeled Pb2+ ions showed that Pb2+ ions bind the native protein in a molar ratio of Pb/protein of 1:5 with moderate inhibition of its biochemical activity. The 4 g-atoms of Zn per mol present in the native enzyme may be removed by dialysis against EDTA. The inactive apoenzyme is capable of incorporating Pb2+ ions in a Pb/protein molar ratio of 2:1, giving a lead-protein complex still enzymatically active also when genetic material, such as nucleotides or DNA, has been used a a substrate. The reconstituted lead-protein is capable of binding Zn2+ ions without any release of the Pb2+ ions and with an increase in the catalytic activity of only 10-15%. The absence of Zn in the inactive apoenzyme as well as in the reconstituted lead-protein, the incorporation of Pb2+ ions in stoichiometric amounts in the apoenzyme, and the weak influence of the Zn2+ ions on the enzymatic assay of the lead-enzyme suggest that lead ions partially reactivate the calf intestine alkaline phosphatase apoenzyme.

Alkaline Phosphatase↗
PubMed1982

Cloning of alkaline phosphatase isozyme gene (iap) of Escherichia coli.

In Escherichia coli three major alkaline phosphatase isozymes are formed by molecular conversions depending on physiological conditions. A chromosomal gene, iap, is responsible for alkaline phosphatase isozyme conversion and is assumed to code for a proteolytic enzyme removing the arginine residue(s) from the N-terminal position of alkaline phosphatase subunits. A chromosomal fragment which complemented the Iap- phenotype was cloned into pBR322 by a shotgun method. Transducing phage lambda iap was constructed in vitro from the chromosomal fragment containing the iap gene and lambda tna DNA. The integration site of the phage on chromosome was identified as the iap locus by P1 transduction, which meant that the cloned chromosomal DNA contained authentic iap gene. The restriction map of the hybrid plasmid was constructed. Based upon this information, several iap deletion plasmids as well as smaller iap+ plasmids were constructed. Analysis of the phenotypes conferred by these plasmids enabled us to locate iap gene within a 2-kb segment of the cloned DNA. The cells carrying the iap+ plasmid showed very efficient isozyme conversion even in medium containing arginine, an inhibitor for the isozyme conversion. This indicates overproduction of the iap gene product.

Alkaline Phosphatase↗
PubMed1992

Amplified assay of alkaline phosphatase using flavin-adenine dinucleotide phosphate as substrate.

A simple to use, robust, quantitative, and extremely sensitive colorimetric assay for alkaline phosphatase (EC 3.1.3.1), designed to be used as a detection system in diagnostic assays employing antibodies or gene probes, is described. This technology is based on the novel principle of prosthetogenesis, according to which a purpose-designed substrate (a prosthetogen) for a primary analyte-linked enzyme label is hydrolyzed to produce a prosthetic group for a detector enzyme system. The prosthetogen employed here is a derivative of FAD which is phosphorylated at the 3'-position of the ribose ring (FADP), the label enzyme is alkaline phosphatase, and the detector is a D-amino-acid oxidase/horseradish peroxidase-coupled system. Essentially each turnover of every molecule of alkaline phosphatase produces a molecule of D-amino-acid oxidase for detection. Thus enormous amplification of the initial signal is achieved in short time periods because of the relatively high turnover number of alkaline phosphatase for FADP. The system can be formatted as a stable, preformed, freeze-dried preparation containing all analytical components, which is reconstituted simply by addition of buffer solution. This methodology can quantitate less than 0.1 amol of alkaline phosphatase in 30 min at 25 degrees C using microtiter plates.

Alkaline Phosphatase↗
PubMed1999

A general method for rapid purification of soluble versions of glycosylphosphatidylinositol-anchored proteins expressed in insect cells: an application for human tissue-nonspecific alkaline phosphatase.

A soluble form of tissue-nonspecific alkaline phosphatase was purified to apparent homogeneity from the culture media of Sf9 cells which had been infected with recombinant baculoviruses encoding human tissue-nonspecific alkaline phosphatase (TNSALP). To facilitate purification, an oligonucleotide consisting of 6 tandem codons for histidine and a stop codon was engineered into the TNSALP cDNA. The molecular mass of the enzyme purified through a nickel-chelate column was estimated to be 54 kDa by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis. That of the native enzyme was 90 kDa as estimated by gel filtration, indicating that the purified soluble TNSALP is dimeric. The enzyme was used for production of antibodies specific for human TNSALP. Immunoblotting analysis showed a single 80-kDa band in the cell homogenate prepared from Saos-2 (human osteosarcoma) cells. However, upon digestion with peptide: N-glycosidase F, the 80-kDa TNSALP of human origin and the soluble enzyme of insect origin migrated to the same position on SDS-polyacrylamide gel, indicating that the size difference between the two enzymes is ascribed to N-linked oligosaccharides. The antibodies prepared against the purified TNSALP were found to be useful also for immunoprecipitation and immunofluorescence studies.

Alkaline Phosphatase↗
PubMed1999

Measurement of serum bone-specific alkaline phosphatase activity in cynomolgus macaques.

Serum levels of bone-specific alkaline phosphatase activity (B-ALP) in cynomolgus monkeys were evaluated as an index of elevated bone turnover following ovariectomy. The enzyme immunoassay 96-well microtiter plate B-ALP assay, developed by Metra Biosystems (Mountain View, CA) for human use, was employed and compared with a standard automated assay measuring total serum levels of alkaline phosphatase activity (T-ALP). The B-ALP assay was first validated for use in these monkeys. Ovariectomy led to increased bone turnover as indicated by approximately 2-fold higher activity in both assays and this elevation was inhibited by daily estradiol administration. Although both assays provided generally similar results, several monkeys were observed to have greatly elevated values of T-ALP but not B-ALP. This discrepancy is believed to result from high levels of the liver isoform of alkaline phosphatase in monkeys with hepatic dysfunction, which are not detected by the B-ALP assay.

Alkaline Phosphatase↗
PubMed1977

[Leukocyte alkaline phosphatase in epidemic hepatitis].

The carried out investigations on 70 patients with epidemic hepatitis, 52 of them treated with prednisolon and 18-symptomatically revealed the following: the normal alkaline phosphatase, established prior to the treatment, was elevated with the applied prednisolon treatment and showed no significant alteration in the patients without cortico-therapy. No correlation was found between leukocyte alkaline phosphatase and serum alkaline phosphatase transaminase, serum bilirubin and thymol test. No relationship was found between the severity of the ailment course and the leukocyte alkaline phosphatase.

Adolescent↗
PubMedDate not supplied

Histochemical changes in acid and alkaline phosphatase activities in the growing follicles and corpora lutea of the rat ovary.

Changes in acid and alkaline phosphatase activities are studied histochemically in different components of the growing follicles and corpora lutea of different generations. Theca cells of the growing follicles showed strong acid phosphatase activity as compared to that observed in the oocyte and granulosa cells. Alkaline phosphatase activity is localized only in the theca interna cells of growing follicles. However, after ovulation with the formation of corpora lutea, the granulosa lutein cells also showed this activity. Changes in the histochemical distribution of the acid and alkaline phosphatases in the follicles and corpora lutea are discussed in relation to folliculogenesis and corpus luteum and regression.

Acid Phosphatase↗
PubMed1978

Induction of alkaline phosphatase activity in HeLa cells by choline chloride.

Choline chloride produced a dose-dependent induction of alkaline phosphatase activity in HeLa cells. At the highest concentration tested, 40 mM, there was a 5- to 7-fold increase in alkaline phosphatase activity, a significantly greater induction than that produced by equiosmolar additions of either NaCl or sucrose. Enzyme activity was higher than control values by 24 hr after the addition of the salt, although the largest increases in activity occurred between 36 and 72 hr. The induction of alkaline phosphatase activity by choline chloride could be inhibited in a dose-dependent manner by the simultaneous addition of either caffeine or theophylline. At comparable concentrations of inhibitor, the magnitude of the inhibition of the induction produced by choline chloride was greater than that observed when the xanthines were used to inhibit the induction by either 5-iodo-2'-deoxyuridine or NaCl. Choline chloride, like NaCl, produced a proportionately greater increase in the heat-stable rather than the heat-labile form of alkaline phosphatase activity.

Alkaline Phosphatase↗
PubMed1978

The role of Zn(II) in calf intestinal alkaline phosphatase studied by the influence of chelating agents and chemical modification of histidine residues.

Alkaline phosphatase from calf intestine (orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1) is reversibly inhibited at pH 8.0 by incubation with chelating agents. Complete reactivation may be achieved by stoichiometric addition of Zn2+. Atomic absorption spectrometry was used to demonstrate the linear correlation between Zn2+ content and degree of reactivation. The reversibly inhibited enzyme contained 1 Zn2+ per subunit whereas 2 Zn2+ were found in both the reactivated and the native enzyme. At more alkaline pH-values, inactivation by chelating agents becomes irreversible; under such conditions the inactivated alkaline phosphatase still contains 1 Zn2+ per subunit. The conformational changes resulting from the loss of Zn2+ and leading to irreversible inactivation were investigated by optical rotatory dispersion, immunological techniques, and ultraviolet and fluorescence spectroscopy. Azocoupling of the alkaline phosphatase with diazonium-1-H-tetrazole and Zn2+ content measurement of azocoupled enzyme probes indicated that 2 histidine residues per subunit are involved in binding of the catalytically important Zn2+.

Alkaline Phosphatase↗
PubMed1988

Conformational studies of bovine alkaline phosphatase in hydrophobic interaction and size-exclusion chromatography with linear diode array and low-angle laser light scattering detection.

Alkaline phosphatase has been studied in hydrophobic interaction chromatography (HIC), using a bonded C1-ether phase on a silica gel support, together with an aqueous salt gradient. Its behavior under various gradient elution conditions has demonstrated good chromatographic performance and retention of enzymatic activity under aqueous conditions. It has now been studied using linear photodiode array (LDA) spectroscopy in combination with low-angle laser light scattering (LALLS) in gradient elution HIC. HIC-LALLS permitted the use of routine salt gradients for collection of molecular weight information, despite small changes in the baseline, via computerized baseline subtraction. Size-exclusion chromatography (SEC)-LALLS measurements, under various isocratic conditions, meant to mimic HIC elution, have indicated the presence of monomer/dimer, dimer/trimer, or mainly trimer. aggregates of alkaline phosphatase can also be detected under salt gradient HIC conditions, but at lower levels relative to the monomer. This paper also describes the behavior of alkaline phosphatase when detected using LDA under various chromatographic, temperature, and concentration (injected) conditions. The results indicate a facile equilibrium of at least two monomeric forms of alkaline phosphatase of the same molecular weight, which change relative populations as a function of operational conditions. Most interesting is the suggestion that alkaline phosphatase undergoes rapid conformational interconversions on the chromatographic detection time scales, and that these interconverting conformations, concentration dependent, produce a novel dual wavelength ratioing, viz., a pseudo-Gaussian peak mimicking the chromatographic elution profile at either wavelength. The reasons for these observations and their possible use in future high-performance liquid chromatographic biopolymer studies are discussed and described.

Alkaline Phosphatase↗