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Isolation, expression and characterization of a human apolipoprotein B 100-specific cDNA clone
Biological Chemistry Hoppe-Seyler
|October 1, 1986
Summary
Researchers isolated and characterized a human apolipoprotein B 100 (apo B 100) cDNA clone. This clone aids in understanding apo B 100 gene expression and protein structure.
Area of Science:
- Molecular Biology
- Genetics
- Biochemistry
Background:
- Apolipoprotein B 100 (apo B 100) is a critical protein in lipid metabolism.
- Understanding apo B 100 gene expression is vital for studying related diseases.
Purpose of the Study:
- To isolate and characterize a human apo B 100-specific cDNA clone.
- To analyze the C-terminal coding region and 3'-nontranslated region of apo B 100.
Main Methods:
- cDNA library screening using immunoscreening with specific antibodies.
- Nucleotide sequencing of the apo B 100 cDNA insert.
- Northern blot hybridization to analyze mRNA expression.
Main Results:
- A human apo B 100 cDNA clone (lambda gt-B1) with a 1321 bp insert was isolated.
- The clone encodes the C-terminal 345 amino acids and the 3'-nontranslated region of apo B 100.
- The nucleotide sequence confirmed partial identity with protein sequencing data and detected 20-22 kb mRNA in adult human liver.
Conclusions:
- The characterized apo B 100 cDNA clone provides a valuable tool for further molecular and genetic studies.
- This research contributes to the understanding of apo B 100 synthesis and regulation.