high molecular weight alkaline phosphatase changes following animal copper treatment
نویسندگان
چکیده
conclusions the elevation of hmw-alp activity in cu treated animal suggests the occurrence of biliary disease. this may be used as a biomarker for the diagnosis of copper toxicity. results obtained data showed that with increasing administration of copper, the alp activity was elevated significantly. in comparison with the control group the elevations were between 20%-56% using gel filtration chromatography. it was found that the elevation of serum alp was mostly due to hmw-alp. objectives this study aimed to investigate the relationship between copper treatment and changes in the serum concentration of high molecular weight alkaline phosphatase (hmw-alp). materials and methods male wistar rats were injected intraperitoneally (ip) with copper (cu) as copper chloride (cucl2. 4h2o) 4, 2 and 1 mg/kg for 10, 30 and 60 days respectively. animals were killed at indicated time and blood samples were collected, and sera was separated and used for alkaline phosphatase activity determinations and also for isoenzymes gel filtration chromatography and sephacryl s-300 was used. background although trace amounts of copper (cu) are necessary to maintain proper body functions, the excess amount can contribute to the development of hepatic dysfunction.
منابع مشابه
changes in rat serum high molecular weight alkaline phosphatase following phenobarbital treatment
متن کامل
Changes in serum, liver, and brain high and low molecular weight alkaline phosphatase following manganese toxicity in rats
Changes in serum, liver, and brain high and low molecular weight alkaline phosphatase following manganese toxicity in rats S. M. Mirhashemi a; A. A. Moshtaghie b; M. Ani b; M. -H. Aarabi a a Faculty of Medicine, Biochemistry and Nutrition Department, Kashan University of Medical Sciences, Kashan, Iran b Faculty of Pharmacy, Clinical Biochemistry Department, Isfahan University of Medical Science...
متن کاملplancental alkaline phosphatase changes in hydatiform mole
introduction: this study was performed to establish a complementary method to the diagnosis of complete hydatidiform mole and its differentiation from the other cases of gestational trophoblastic disease by measuring the total (alp) and placental alkaline phosphatase (plap) specific activity. materials and methods: serum and tissue extracts from 13 patients, 13 normal non-pregnant and 30 pregna...
متن کاملNeutrophile Alkaline Phosphatase Changes in Tularemia
With the technical assistance of Sophie Shepel and Ray F. Long T DECADES AGO, Wachstein’ called attention to an increase in alkaline phosphatase (AP) activity of human neutrophilic leukocytes during bacterial infections. Enzyme activity within individual cells as well as the number of cells with detectable enzyme were markedly increased, an observation confirmed by others.27 Infection-induced r...
متن کاملThe release of high-molecular-weight alkaline phosphatase and leucine aminopeptidase into the media of cultured human cells.
Using exclusion from Sepharose 4B as our criterion, we have found a high-molecular-weight form of alkaline phosphatase and of leucine aminopeptidase which are released into the culture media by the FL amnion cell line. A low-molecular-weight form of leucine aminopeptidase is also found to contribute to the total levels of this enzyme in the media. The levels of these enzymes increased during th...
متن کاملIsolation and molecular identification of bacteria producing alkaline phosphatase enzyme from environmental sources
Alkaline phosphatase (ortho phosphate, monoester hydrolase phosphoinositide E. C. 3.1.3.1) is a non-specific metalloproteinase enzyme that is located inside periplasmic space of bacteria. This enzyme is used to measure freshwater sediment in genetic engineering for cleaning water. Isolation and molecular identification of the bacteria producing alkaline phosphatase and comparison of its product...
متن کاملمنابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
avicenna journal of medical biochemistryجلد ۲، شماره ۱، صفحات ۰-۰
کلمات کلیدی
میزبانی شده توسط پلتفرم ابری doprax.com
copyright © 2015-2023