Macromolecular alkaline phosphatase and an immunoglobulin G that inhibited alkaline phosphatase in a patient's serum.

1983 ◽  
Vol 29 (2) ◽  
pp. 375-378 ◽  
Author(s):  
H Nakagawa ◽  
K Umeki ◽  
K Yamanaka ◽  
N Kida ◽  
S Ohtaki
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Immunoglobulin G ◽  
Significant Loss ◽  
Placental Alkaline Phosphatase ◽  
Type Ii ◽  
Intestinal Alkaline Phosphatase ◽  
Adult Type ◽  
Heat Stable

Abstract Macromolecular alkaline phosphatase (EC 3.1.3.1) was found in the serum of a patient suffering from myasthenia gravis (adult type II) complicated with thymoma, and was shown by immunoelectrophoresis to be bound to immunoglobulins A and G (IgG). Placental alkaline phosphatase, complexed with either the patient's serum or IgG purified from the patient's serum, remained at the origin on electrophoresis, with significant loss of activity. Intestinal alkaline phosphatase, complexed with either the patient's serum or the patient's IgG, migrated to a position similar to that of the macromolecular alkaline phosphatase in the patient's serum on electrophoresis. About 50% of the placental alkaline phosphatase activity was inhibited with 0.1-0.2 g of the patient's IgG per liter, but 6.93 g of the IgG per liter was required for about 20% inhibition of the intestinal alkaline phosphatase activity. The complex of intestinal alkaline phosphatase with the patient's IgG was fairly heat stable. From these results, we concluded that the macromolecular alkaline phosphatase in the patient's serum consisted of intestinal alkaline phosphatase and IgG that was specific for placental alkaline phosphatase.

scholarly journals Tissue alkaline phosphatase activity and expression in an experimental infant swine model of cardiopulmonary bypass with deep hypothermic circulatory arrest

2020 ◽  
Author(s):  
Ludmila Khailova ◽  
Justin Robison ◽  
James Jaggers ◽  
Richard Ing ◽  
Scott Lawson ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Cardiac Surgery ◽  
Cardiopulmonary Bypass ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Circulatory Arrest ◽  
Deep Hypothermic Circulatory Arrest ◽  
Hypothermic Circulatory Arrest ◽  
Swine Model ◽  
Intestinal Alkaline Phosphatase

Abstract Background: Infant cardiac surgery with cardiopulmonary bypass results in decreased circulating alkaline phosphatase that is associated with poor post-operative outcomes. Bovine intestinal alkaline phosphatase infusion represents a novel therapy for post-cardiac surgery organ injury. However, the effects of cardiopulmonary bypass and bovine-intestinal alkaline phosphatase infusion on tissue-level alkaline phosphatase activity/expression are unknown.Methods: Infant pigs (n=20) underwent cardiopulmonary bypass with deep hypothermic circulatory arrest followed by four hours of intensive care. Seven control animals underwent mechanical ventilation only. Cardiopulmonary bypass/deep hypothermic circulatory arrest animals were given escalating doses of bovine intestinal alkaline phosphatase infusion (0-25U/kg/hr; n=5/dose). Kidney, liver, ileum, jejunum, colon, heart and lung were collected for measurement of tissue alkaline phosphatase activity and mRNA.Results: Tissue alkaline phosphatase activity varied significantly across organs with the highest levels found in the kidney and small intestine. Cardiopulmonary bypass with deep hypothermic circulatory arrest resulted in decreased kidney alkaline phosphatase activity and increased lung alkaline phosphatase activity, with no significant changes in the other organs. Alkaline phosphatase mRNA expression was increased in both the lung and the ileum. The highest dose of bovine intestinal alkaline phosphatase resulted in increased kidney and liver tissue alkaline phosphatase activity.Conclusions: Changes in alkaline phosphatase activity after cardiopulmonary bypass with deep hypothermic circulatory arrest and bovine intestinal alkaline phosphatase delivery are tissue specific. Kidneys, lung, and ileal alkaline phosphatase appear most affected by cardiopulmonary bypass with deep hypothermic circulatory arrest and further research is warranted to determine the mechanism and biologic importance of these changes.

Non-thermal effects of 0.1 THz radiation on intestinal alkaline phosphatase activity and conformation

2019 ◽  
Vol 28 (12) ◽  
pp. 128702
Author(s):  
Xin-Xin Zhang ◽  
Ming-Xia He ◽  
Yu Chen ◽  
Cheng Li ◽  
Jin-Wu Zhao ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Thermal Effects ◽  
Thz Radiation ◽  
Intestinal Alkaline Phosphatase

scholarly journals Differential determination of the heat-stable alkaline phosphatase activity in serum.

1982 ◽  
Vol 30 (6) ◽  
pp. 2105-2109 ◽  
Author(s):  
KAZUYUKI HIRANO ◽  
YUICHI IIIZUMI ◽  
MAMORU SUGIURA ◽  
JUN MIYAZAKI ◽  
KAZUMASA MIKI ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Heat Stable

scholarly journals Isolation and characterization of a Chinese hamster ovary (CHO) mutant defective in the second step of glycosylphosphatidylinositol biosynthesis

1996 ◽  
Vol 313 (1) ◽  
pp. 253-258 ◽  
Author(s):  
Victoria L. STEVENS ◽  
Hui ZHANG ◽  
Michelle HARREMAN
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Chinese Hamster Ovary ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Second Step ◽  
Molecular Defect ◽  
Placental Alkaline Phosphatase ◽  
Isolation And Characterization

Mutant cell lines defective in the biosynthesis of glycosylphosphatidylinositol (GPI) described to date were isolated by selecting cells which no longer expressed one or more endogenous GPI-anchored proteins on their surface. In this study, a new mutant in this pathway was isolated from ethylmethanesulphonate-mutagenized Chinese hamster ovary cells stably transfected with human placental alkaline phosphatase (PLAP) as a marker of GPI-anchored proteins. A three-step protocol was employed. In the first step, cells with decreased surface expression of PLAP were selected by four rounds of complement-mediated lysis with an anti-(alkaline phosphatase) antibody. The surviving cells were cloned by limiting dilution and those with low levels of total alkaline phosphatase activity were selected in the second step. Finally, the ability of each clone to synthesize the first three intermediates in GPI biosynthesis in vitro was assessed to determine which cells with low alkaline phosphatase activity harboured a defect in one of these reactions. Of 230 potential mutants, one was defective in the second step of GPI biosynthesis. Microsomes from this mutant, designated G9PLAP.85, were completely unable to deacetylate either endogenous GlcNAc-phosphatidylinositol (PI) synthesized from UDP[6-3H]GlcNAc or exogenous GlcNAc-PI added directly to the membranes. Complementation analysis with the Thy-1-deficient murine lymphoma cells demonstrated that G9PLAP.85 has a molecular defect distinct from these previously described mutants. Therefore, these results suggest that mutants in GPI biosynthesis could be selected from almost any cell line expressing a GPI-anchored marker protein.

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