THE PURIFICATION OF ALKALINE PHOSPHATASE FROM HUMAN PLACENTA

Q: How can I download an article?

To download an article from SID, first log in to the site, search for the article title, and click on the 'Download Article' option.

Q: How can I download an ISI article?

To download an ISI article on SID, enter the keyword or article title in the search bar, view the relevant results, click on the desired article, and select the 'Download Article' option.

Q: How can I access the SID database?

To access the SID database, visit SID.ir, create an account, and log in to access scientific resources.

Q: Is downloading articles from SID free?

Some articles on SID are available for free, while others require payment. Details are specified on the article's page.

ABERUMAND M.; FARAMARZI B.

مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Journal Paper

Paper Information

Journal: Journal of Sabzevar University of Medical Sciences Year:2002 | Volume:8 | Issue:4 (22) Page(s): 32-39

Download Full-Text

Persian Verion

View:

1,121

Download:

Cites:

Information Journal Paper

Title

THE PURIFICATION OF ALKALINE PHOSPHATASE FROM HUMAN PLACENTA

Author(s)

ABERUMAND M. | FARAMARZI B. | Issue Writer Certificate

Keywords

ALKALINE PHOSPHATASEQ2

HUMAN PLACENTAQ4

CHROMATOGRAPHYQ3

POLYACRYLANIDE DISC GEL ELECTROPHORESISQ4

Abstract

ALKALINE PHOSPHATASE, an orthophosphoric monoester phosphohydrolase Ec 3.1. 3.1., is a glycoprotein dimer. It is active in alkaline PH and needs mg2+ ion as an activator. This membrane-bound enzyme is widely distributed in nature. In this study, it was purified from HUMAN PLACENTA in seven steps. Placenta was homogenated and the enzyme was extracted through following steps: Butanol extraction, filtration on sephadex G200, ammonium sulfate precipitation, aceton precipation and DEAE cellulose CHROMATOGRAPHY with a gradient of sodium chloride. A peak of the enzyme activity at sodium chloride concentrations of 0.087 to 0.093 mg was observed on DEAE cellulose CHROMATOGRAPHY. The specific activity of the enzyme and purification factor were observed to be 209.9 U/mg and 611.8 respectively. At the final steps of preparative electrophoresis, the purified enzyme was. subjected to polyacrylamide disc gel electrophoresis. P-nitrophenyl phosphate was used, instead of N-naphthyl phosphate, to stain ALKALINE PHOSPHATASE. The appearance of a yellaw band proved the purification of the enzyme.

Cites

STUDY OF THE NEW HUMAN MOLEHYDATIFORM ALKALINE PHOSPHATASE

References

No record.

Cite

APA: Copy

ABERUMAND, M., & FARAMARZI, B.. (2002). THE PURIFICATION OF ALKALINE PHOSPHATASE FROM HUMAN PLACENTA. JOURNAL OF SABZEVAR UNIVERSITY OF MEDICAL SCIENCES, 8(4 (22)), 32-39. SID. https://sid.ir/paper/81894/en

Vancouver: Copy

ABERUMAND M., FARAMARZI B.. THE PURIFICATION OF ALKALINE PHOSPHATASE FROM HUMAN PLACENTA. JOURNAL OF SABZEVAR UNIVERSITY OF MEDICAL SCIENCES[Internet]. 2002;8(4 (22)):32-39. Available from: https://sid.ir/paper/81894/en

IEEE: Copy

M. ABERUMAND, and B. FARAMARZI, “THE PURIFICATION OF ALKALINE PHOSPHATASE FROM HUMAN PLACENTA,” JOURNAL OF SABZEVAR UNIVERSITY OF MEDICAL SCIENCES, vol. 8, no. 4 (22), pp. 32–39, 2002, [Online]. Available: https://sid.ir/paper/81894/en

Related Journal Papers