Quantitative determination of surface concentration of human apolipoprotein H with capillary electrophoresis
The phospholipid monolayer at an air/water interface is widely used to mimic the biological membrane. The dynamic process of the protein or peptide interacting with lipid molecules can be reflected in the change in surface pressure of the monolayer. But the conventional method used to measure the su...
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Published in | IUBMB life Vol. 49; no. 5; p. 437 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
England
01.05.2000
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Abstract | The phospholipid monolayer at an air/water interface is widely used to mimic the biological membrane. The dynamic process of the protein or peptide interacting with lipid molecules can be reflected in the change in surface pressure of the monolayer. But the conventional method used to measure the surface pressure change gives results that cannot easily be correlated with the contribution of a single protein molecule. Previously, measuring the surface concentration of the protein molecules at the air/water interface has required the protein to be labeled with radioactivity or fluorescence. Here, a new method using capillary electrophoresis is introduced to measure the surface concentration of the protein. The results show at least two advantages of the new method: The numerical results of protein concentration can be obtained in a more precise and rapid way; and there is no need to label the protein sample or to build a special monolayer setup. |
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AbstractList | The phospholipid monolayer at an air/water interface is widely used to mimic the biological membrane. The dynamic process of the protein or peptide interacting with lipid molecules can be reflected in the change in surface pressure of the monolayer. But the conventional method used to measure the surface pressure change gives results that cannot easily be correlated with the contribution of a single protein molecule. Previously, measuring the surface concentration of the protein molecules at the air/water interface has required the protein to be labeled with radioactivity or fluorescence. Here, a new method using capillary electrophoresis is introduced to measure the surface concentration of the protein. The results show at least two advantages of the new method: The numerical results of protein concentration can be obtained in a more precise and rapid way; and there is no need to label the protein sample or to build a special monolayer setup. |
Author | Luo, G Ru, Q Sui, S Sun, Y Wang, S |
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SubjectTerms | beta 2-Glycoprotein I Cell Membrane - metabolism Dimyristoylphosphatidylcholine - metabolism Electrophoresis, Capillary - methods Glycoproteins - biosynthesis Humans Indicators and Reagents - metabolism Membranes, Artificial Phosphatidylglycerols - metabolism Phospholipids - metabolism Time Factors |
Title | Quantitative determination of surface concentration of human apolipoprotein H with capillary electrophoresis |
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