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Rat apolipoprotein B differs in solubility properties from human apolipoprotein B.
V S Kamanna1, D L Stiers, D M Lee
1Lipoprotein and Atherosclerosis Research Program, Oklahoma Medical Research Foundation, Oklahoma City 73104.
Biochimica Et Biophysica Acta
|March 12, 1990
Summary
Delipidized rat apolipoprotein B (ApoB) showed surprising solubility in aqueous buffers, unlike human ApoB. This suggests potential structural differences between rat and human ApoB, impacting protein behavior.
Area of Science:
- Biochemistry
- Proteomics
- Comparative Biology
Background:
- Apolipoprotein B (ApoB) is typically insoluble in aqueous solutions without denaturing agents.
- Understanding ApoB solubility is crucial for lipoprotein metabolism research.
Purpose of the Study:
- To investigate the solubility of delipidated rat apolipoprotein B (ApoB) in aqueous buffers.
- To compare the solubility of rat ApoB with human ApoB.
Main Methods:
- Total delipidation of rat plasma low-density lipoproteins.
- Solubility assay in N-ethylmorpholine acetate buffer (pH 7.3).
- Analysis using SDS-polyacrylamide gel electrophoresis, immunoblotting, and electron microscopy.
Main Results:
- A significant portion (28.2 +/- 3.0%) of delipidated rat ApoB demonstrated direct solubility in the aqueous buffer.
- This solubility was not observed for human ApoB under identical conditions.
- SDS-PAGE, immunoblotting, and electron microscopy confirmed the presence and solubility of rat ApoB.
Conclusions:
- Rat ApoB exhibits unique aqueous solubility after delipidation, contrasting with human ApoB.
- These findings suggest inherent structural variations between rat and human ApoB.
- The observed solubility difference may have implications for understanding lipoprotein structure and function across species.