Biochemical and Kinetic Study for the partially purified Lecithin: Cholesterol acyltransferase from serum cardiovascular disease
DOI:
https://doi.org/10.25130/tjps.v25i2.233Keywords:
Separation, Enzyme, Lecithin: Cholesterol acyltransferase (LCAT)Abstract
The study includes partial purification of Lecithin: Cholesterol acyltransferase (LCAT) from the blood serum of a person suffering from atherosclerosis. Several techniques were applied including ammonium sulphate precipitation, dialysis, ion exchange chromatography and electrophoresis. It was found that LCAT has one isoenzyme and the highest activity was (1073.46 × 10-3) unit/ml and a molecular weight of 62 KDa. The study also deals with characterizing of LCAT. It was found that the optimum pH and temp. of the enzyme were 7 and 35ºC.
Downloads
Published
How to Cite
License
Copyright (c) 2022 Tikrit Journal of Pure Science
This work is licensed under a Creative Commons Attribution 4.0 International License.
Tikrit Journal of Pure Science is licensed under the Creative Commons Attribution 4.0 International License, which allows users to copy, create extracts, abstracts, and new works from the article, alter and revise the article, and make commercial use of the article (including reuse and/or resale of the article by commercial entities), provided the user gives appropriate credit (with a link to the formal publication through the relevant DOI), provides a link to the license, indicates if changes were made, and the licensor is not represented as endorsing the use made of the work. The authors hold the copyright for their published work on the Tikrit J. Pure Sci. website, while Tikrit J. Pure Sci. is responsible for appreciate citation of their work, which is released under CC-BY-4.0, enabling the unrestricted use, distribution, and reproduction of an article in any medium, provided that the original work is properly cited.
