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Molecular cloning and sequence analysis of full-length cDNA coding for mouse contrapsin
Y Suzuki1, K Yamamoto, H Sinohara
1Department of Biochemistry, Kinki University School of Medicine, Osaka.
Journal of Biochemistry
|September 1, 1990
Summary
Researchers isolated mouse contrapsin cDNA clones from a liver library. Sequence analysis revealed a 418-amino acid protein with 64% homology to human alpha-1-antichymotrypsin.
Area of Science:
- Molecular Biology
- Genetics
- Biochemistry
Background:
- Contrapsin is a protein found in mouse liver.
- Understanding its genetic makeup is crucial for biological research.
Purpose of the Study:
- To isolate and characterize cDNA clones encoding mouse contrapsin.
- To determine the full-length sequence and identify key regulatory elements.
Main Methods:
- Construction of a mouse liver cDNA library in lambda gt11 expression vector.
- Isolation and sequencing of overlapping cDNA clones using M13 vector methods.
- Analysis of open reading frame, amino acid sequence, and polyadenylation signals.
Main Results:
- Four overlapping cDNA clones encoding contrapsin were successfully isolated.
- The contrapsin cDNA contains an open reading frame of 1,254 bases, coding for 418 amino acids.
- The deduced amino acid sequence shows 64% homology to human alpha-1-antichymotrypsin, and distinct polyadenylation signals were identified.
Conclusions:
- The study provides the complete nucleotide and amino acid sequence of mouse contrapsin.
- Identified sequence homology suggests functional similarities between mouse contrapsin and human alpha-1-antichymotrypsin.
- The presence of multiple polyadenylation signals indicates potential for alternative mRNA processing.