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High homology is present in the primary structures between murine senile amyloid protein (ASSAM) and human
Abstract:
The primary structure of a murine senile amyloid protein (ASSAM) was determined. The protein consists of a single polypeptide chain of 78 amino acid residues. The amino-terminus is blocked with pyrrolidone-carboxylic acid. The sequence differs from that of the known murine amyloid A protein and is highly homologous to human apolipoprotein (apo) A-II. The result indicates that the putative precursor of the senile amyloid protein is apo A-II in mice.
Insights
Researchers determined the primary structure of a murine senile amyloid protein (ASSAM), finding it homologous to human apolipoprotein A-II. This suggests apolipoprotein A-II is the precursor for ASSAM in mice.
Area of Science:
- Biochemistry
- Molecular Biology
- Gerontology
Background:
- Senile amyloid protein (ASSAM) is a key component in age-related amyloid deposits.
- Understanding the molecular basis of ASSAM is crucial for studying aging and associated diseases.
Purpose of the Study:
- To determine the primary amino acid sequence of murine senile amyloid protein (ASSAM).
- To identify the precursor protein of ASSAM in mice.
Main Methods:
- Amino acid sequencing of the purified ASSAM protein.
- Bioinformatic analysis for sequence homology comparison.
Main Results:
- The primary structure of ASSAM was elucidated, revealing a 78-amino acid polypeptide chain.
- The amino-terminus of ASSAM is blocked by pyrrolidone-carboxylic acid.
- ASSAM sequence shows significant homology to human apolipoprotein (apo) A-II, differing from murine amyloid A protein.
Conclusions:
- Murine senile amyloid protein (ASSAM) is structurally related to apolipoprotein A-II.
- Apolipoprotein A-II is identified as the likely precursor of ASSAM in mice, providing insights into amyloid formation in aging.