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Amino acid sequence of rabbit apolipoprotein E
B R Lee1, J M Miller, C Y Yang
1Department of Medicine, Baylor College of Medicine, Houston, TX.
Journal of Lipid Research
|January 1, 1991
Summary
Rabbit apolipoprotein E (apoE) sequence analysis reveals 294 amino acids. Its high homology to human apoE facilitates in vitro studies relevant to human lipid metabolism.
Area of Science:
- Biochemistry
- Molecular Biology
- Proteomics
Background:
- Apolipoprotein E (apoE) plays a crucial role in lipid metabolism and transport.
- Understanding the precise amino acid sequence of apoE is essential for studying its function and structure.
- Rabbit apoE serves as a model for studying human apoE due to potential similarities.
Purpose of the Study:
- To determine the complete amino acid sequence of rabbit apolipoprotein E (apoE).
- To compare the determined rabbit apoE sequence with the sequence inferred from cDNA.
- To assess the homology between rabbit and human apoE sequences for potential in vitro studies.
Main Methods:
- Protein cleavage using cyanogen bromide, endoproteinase AspN, and Staphylococcus aureus V8 protease.
- N-terminal and C-terminal residue identification through sequence analysis.
- Amino acid sequencing of 294 residues to determine molecular weight and sequence homology.
Main Results:
- The complete amino acid sequence of rabbit apoE was elucidated, comprising 294 residues with a molecular weight of 33,684 Da.
- The determined protein sequence corrected discrepancies found in the cDNA-inferred sequence.
- Rabbit apoE exhibits 80% homology with human apoE, a higher degree than previously inferred from cDNA.
Conclusions:
- The high amino acid sequence homology between rabbit and human apoE suggests similar physiological properties.
- Rabbit apoE is a suitable model for in vitro studies relevant to human apoE, overcoming limitations of human protein availability.