Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.1.3.1 (alkaline phosphatase)
47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In human serum, polymorphism of apoA-II predominantly in HDL3 could be demonstrated. HDL3-apoA-II was composed of four isoproteins, each with a molecular weight of 8600 (reduced form) and identical immunological properties. The isoproteins are designated apoA-II-1 (pI 5.16), apoA-II-2 (pI 4.89) corresponding to the already known apoA-II monomer band, apoA-II-3 (pI 4.58), and apoA-II-4 (pI 4.31). The amino acid compositions of the A-II isoproteins were virtually identical with the published data for apoA-II. Treatment with acid phosphatase, alkaline phosphatase, or neuraminidase before electrophoresis did not alter the apoA-II pattern. The apoA-II isoprotein pattern was studied in ten male and ten female normolipidemic volunteers, in two patients with Tangier disease, and in three patients with abetalipoproteinemia. The isoelectric focusing patterns of apoA-II appeared virtually identical in all subjects. However, in Tangier disease, due to the low apo-A-II concentration, only apoA-II-1 and apoA-II-2 were detectable, and in abetalipoproteinemia a different relative distribution pattern of the individual isoforms was found as compared to normal HDL3. Our studies indicate that apoA-II, similar to apoA-I, exists in several isoforms. The relationship of these isoforms to each other is at present unclear. They may originate from relatively basic isoproteins that are modified in charge by post-translational processes such as proteolytic cleavage, sequential deamidation, or other mechanisms.
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PMID:Isoproteins of human apolipoprotein A-II: isolation and characterization. 663 Dec 30

Arylsulfatase A, B and an anionic form of B were separated by DEAE-cellulose column chromatography from the brains of man, monkey, rabbit, rat and chicken. The relative proportion of brain arylsulfatases differed from one species to the other. The anionic form of arylsulfatase B was a minor component as compared to arylsulfatase A or B in human and monkey brains while it was a major component in rat and chicken brains. Anionic arylsulfatase B was found in fetal human brains and in newborn monkey brain. In the rat brain, the activities of arylsulfatases A and anionic B showed an increasing trend during development, reaching a peak around 20 days after birth, without any change in their proportions. Treatment with Escherichia coli alkaline phosphatase resulted in the conversion of a major portion (about 70%) of the anionic arylsulfatase B of human and monkey brains into a less charged form which remained unbound to DEAE-cellulose. This conversion by phosphatase was inhibited by inorganic phosphate. Rat and chicken brain anionic arylsulfatase B was not susceptible to alkaline phosphatase. Vibrio cholerae neuraminidase treatment did not significantly affect the charge on anionic arylsulfatase B from any of the species. The results suggested a phosphorylated form of anionic arylsulfatase B exclusively in the primate brain.
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PMID:Anionic forms of brain arylsulfatase B: evidence for a phosphorylated form in man and monkey. 668 Jun 91

An alkaline phosphatase isoenzyme that did not move from the origin in agarose gel electrophoresis was detected in serum from a 51-year-old woman with Hodgkin's disease. Inhibitor and heat-inactivation studies of the patient's serum alkaline phosphatase showed properties resembling those of both liver and bone isoenzymes. No immunoglobulin or high-molecular-mass complexes with the alkaline phosphatase isoenzyme were detected. The relative molecular mass (Mr) of the atypical alkaline phosphatase isoenzyme was 182 000, that of the liver alkaline phosphatase isoenzyme control 170 000. Treatment of both of these isoenzymes with neuraminidase gave a product with an Mr of 140 000. We propose that a post-translational modification increased the carbohydrate content of the liver alkaline phosphatase isoenzyme, thus changing the charge characteristics of the enzyme and decreasing its electrophoretic mobility. We believe this to be the first report of a post-translational modification in a heat-sensitive isoenzyme of alkaline phosphatase.
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PMID:Atypical alkaline phosphatase isoenzyme in serum from a patient with Hodgkin's disease. 671 46

The specific activity of alkaline phosphatase in the rat duodenum increased just prior to birth, leveled off and then increased again at about 20 days after birth. During the postnatal rise in activity the electrophoretic pattern of the enzyme on sodium dodecyl sulphate (SDS) polyacrylamide gels changed from a single activity band to three bands. The changed pattern was identical with that of the adult duodenal enzyme. The fetal- and adult-type enzymes had different sensitivities to neuraminidase, suggesting that there is a significant difference in the sialic acid content of these two forms. This molecular conversion may be necessary for adaptation to eating a solid food diet, because it occurs just before the weaning period.
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PMID:Developmental changeover in rat duodenal alkaline phosphatase. 671 24

Twenty members of a family with adult hypophosphatasia were examined clinically and biochemically. Severe caries causing early loss of permanent teeth was the only clinical symptom which could be attributed to hypophosphatasia. None of them had a history of defective bone mineralization, rachitic skeletal alterations, and recurrent pseudofractures or fractures. An iliac crest bone biopsy of the proposita showed a normal finding corresponding to the age of the patient. Four family members in two subsequent generations were affected, thus suggesting an autosomal dominant inheritance. Their serum and leukocyte alkaline phosphatases were reduced. The phosphoethanolamine (PEA) excretion in the urine was increased to a level which suggests a heterozygote state. The serum alkaline phosphatase activity could be ascribed to the liver isoenzyme fraction. This was shown by polyacrylamide electrophoresis, by inhibition studies with organ-specific inhibitors, heat inactivation, inhibition by antibodies, and treatment with neuraminidase. The proposita had an unexplained, diffuse fatty infiltration of the liver. Thus, not only alterations of bone but also of liver metabolism in hypophosphatasia should be considered. The variety of adult hypophosphatasia described in this paper is characterized by the lack of severe bone abnormalities, the apparently autosomal dominant inheritance, and the reduction of bone and intestinal isoenzyme in the serum. Our study suggests that hypophosphatasia is a heterogeneous disorder which includes both severe and clinically mild forms.
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PMID:Adult hypophosphatasia without apparent skeletal disease: "odontohypophosphatasia" in four heterozygote members of a family. 672 76

A pancreas-specific antigen was identified by immunologic techniques and purified from saline extract of human pancreas. The purified pancreas-specific antigen was shown to be homogeneous by polyacrylamide gel electrophoresis under both denaturing and non-denaturing conditions. It had a molecular weight of 44000 as estimated by gel filtration or sodium dodecyl sulfate-gel electrophoresis, and a sedimentation coefficient of 3.4 S as analyzed by sucrose gradient centrifugation. Pancreas-specific antigen possessed an isoelectric point of 4.9 and migrated to alpha-beta region upon immunoelectrophoresis. By colorimetric assay procedures, pancreas-specific antigen exhibited no enzyme activity, such as amylase, protease, esterase, lipase, acid phosphatase, alkaline phosphatase peroxidase, deoxyribonuclease or ribonuclease. Immunoreactivity of pancreas-specific antigen was sensitive to proteolytic enzymes, perchloric acid and high temperature (70 degrees C, 10 min); but insensitive to neuraminidase or beta-glucosidase. Immunohistochemical staining revealed that pancreas-specific antigen was located in acinar cells of human pancreas. In addition, a higher concentration of pancreas-specific antigen was detected in pancreatic juice than in the saline extract of pancreas. This newly identified pancreas-specific antigen, therefore, may be a useful marker protein in physiological studies of pancreas and pancreatic secretion.
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PMID:Purification and characterization of a human pancreas-specific antigen. 678 69

The D98/AH-2 cell line (a subline of HeLa) expresses a form of alkaline phosphatase (ALP) which closely resembles the adult and fetal intestinal forms of ALP. To characterize this ectopic form of ALP, four monoclonal antibodies were raised against D98/AH-2 ALP, and their binding with ALPs from D98/AH-2 cells, placenta, fetal intestine (meconium), adult intestine, and liver was compared using an electrophoretic titration procedure. The ALPs were either untreated or treated with neuraminidase. All four monoclonal antibodies bound desialated D98/AH-2 ALP most strongly. Adult intestinal ALP, which does not contain sialic acid residues, reacted much more strongly than either sialated or desialated fetal intestinal ALP. Two of the four monoclonal antibodies reacted very weakly or not at all with placental ALP, but two others reacted more strongly with placental ALP than with fetal intestinal ALP. None of the antibodies reacted with liver ALP. From these results, it appears that D98/AH-2 ALP may be a modified form of adult intestinal ALP.
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PMID:Monoclonal antibodies to an ectopically expressed alkaline phosphatase in a human malignant cell line. 684 90

The molecular structure of human foetal intestinal alkaline phosphatase was defined by high-resolution two-dimensional polyacrylamide-gel electrophoresis and amino acid inhibition studies. Comparison was made with the adult form of intestinal alkaline phosphatase, as well as with alkaline phosphatases isolated from cultured foetal amnion cells (FL) and a human tumour cell line (KB). Two non-identical subunits were isolated from the foetal intestinal isoenzyme, one having same molecular weight and isoelectric point as placental alkaline phosphatase, and the other corresponding to a glycosylated subunit of the adult intestinal enzyme. The FL-cell and KB-cell alkaline phosphatases were also found to contain two subunits similar to those of the foetal intestinal isoenzyme. Characterization of neuraminidase digests of the non-placental subunit showed it to be indistinguishable from the subunits of the adult intestinal isoenzyme. This implies that no new phosphatase structural gene is involved in the transition from the expression of foetal to adult intestinal alkaline phosphatase, but that the molecular changes involve suppression of the placental subunit and loss of neuraminic acid from the non-placental subunit. Enzyme-inhibition studies demonstrated an intermediate response to the inhibitors tested for the foetal intestinal, FL-cell and KB-cell isoenzymes when compared with the placental, adult intestinal and liver forms. This result is consistent with the mixed-subunit structure observed for the former set of isoenzymes. In summary, this study has defined the molecular subunit structure of the foetal intestinal form of alkaline phosphatase and has demonstrated its expression in a human tumour cell line.
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PMID:Characterization of human foetal intestinal alkaline phosphatase. Comparison with the isoenzymes from the adult intestine and human tumour cell lines. 688 58

Administration of 1,25-(OH)2D3 to developing 14-day chick embryo gave precocious induction of alkaline phosphatase in 20-day chick embryonic duodenum. 1,25-(OH)-2D3-induced alkaline phosphase involved in changes in Km and Vmax values. Furthermore, polyacrylamide gel disc electrophoresis of n-butanol-solubilized alkaline phosphatase from control and 1,25-(OH)2D3-treated chick embryonic duodenum revealed that 1,25-(OH)2D3 involved the transformation of neuraminidase-resistant fast migrating form to the neuraminidase-sensitive faster migrating one. Scanning electron microscopic data showed that the injection of 1,25-(OH)2D3 stimulated the elongation of duodenal microvilli, although there was no effect on the duodenal absorptive epithelial cell height.
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PMID:Effect of 1,25-dihydroxycholecalciferol on the duodenal villi and alkaline phosphatase in the developing chick embryo. 689 76

Three cell lines of mature T cell origin established from patients with cutaneous T cell lymphoma-leukemia (CTCL) have been found to be constitutive producers of TCGF (L-TCGF). Biologically active L-TCGF can also be eluted from the plasma membranes of these cells. We have compared the biologic and biochemical properties of L-TCGF and TCGF derived from normal lymphocytes (N-TCGF). L-TCGF and N-TCGF share similar biologic activity: both support long-term growth of T cells that have undergone prior lectin or antigen stimulation, and have no effect on unstimulated T cells. However, L-TCGF is a more acidic (pI 4.5 vs 6.5 to 8.0) molecule than N-TCGF and elutes from DEAE-Sepharose at higher salt concentration (0.2 M NaCl vs 0.07 to 0.1 M NaCl). In addition, these two factors display differing mobilities on gel filtration. Treatment of L-TCGF with neuraminidase or alkaline phosphatase does not alter its pI, indicating that enzymatically vulnerable sialic acid or phosphate groups are not involved in the variation. The nature and significance of this biochemical variant remain unknown.
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PMID:A biochemical variant of human T cell growth factor produced by a cutaneous T cell lymphoma cell line. 698 Sep 38


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