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1.
Iranian Journal of Pediatrics. 2010; 20 (3): 269-276
in English | IMEMR | ID: emr-129246

ABSTRACT

There are some controversial studies on effects of anti-epileptic drugs [AEDs] on serum IgG subclasses; however, the role of these medications is still unclear. The aim of this study was evaluation the effects of anti-epileptic drugs on serum concentration of IgG and its subclasses. Serum IgG and IgG subclasses of 61 newly diagnosed epileptic patients were measured at the beginning of monotherapy with carbamazepine, sodium valproate, and phenobarbital, and 6 months later. Measurement of IgG and its subclasses was performed using nephlometry and ELISA techniques, respectively. Reduction of at least one IgG subclass was found in 6 patients 6 months after treatment with AEDs. Among 27 patients receiving carbamazepine, decrease in at least one serum IgG subclass level was found in 5 patients. Among 20 patients using sodium valproate, only one patient showed decrease in IgG2 subclass. None of the 14 patients using phenobarbital revealed significant decrease in IgG subclasses. No infection was seen in the patients with reduction of subclasses. Although in our study, children with selective IgG subclass deficiency were asymptomatic, assessment of serum immunoglobulin levels could be recommended at starting the administration of AEDs and in serial intervals afterward in epileptic patients


Subject(s)
Humans , Male , Female , Immunoglobulin G/drug effects , Epilepsy , Immunoglobulin G/blood , Carbamazepine , Valproic Acid , Phenobarbital
2.
Pakistan Journal of Medical Sciences. 2008; 24 (3): 471-474
in English | IMEMR | ID: emr-89558

ABSTRACT

Study was performed on purification of alkaline phosphatase from Hydatiform mole. The sample of mole Hydatidiform subjects from Taleghani Hospital, Tehran, Iran was studied. An Alkaline phosphatase from Human Hydatidiform mole was purified by a protocol involving solubilization using precipitation by butanol, acetone, Ammonium sulphate, Sephadex G[200], Ion exchange chromatography and preparative electrophoresis. The enzyme was purified 800-fold to apparent homogeneity. This enzyme has 5.2% carbohyrate content. The optimum Temperature and pH were 40 centigrade degree and 10.4, respectively. Human Hydatidiform mole alkaline phosphatase is a novel alkaline phosphatase


Subject(s)
Humans , Hydatidiform Mole/enzymology , Chemical Precipitation , Acetone , Ammonium Sulfate , Dextrans , Chromatography, Ion Exchange , Electrophoresis
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