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[Different primary structure of 2 variants of Friend virus p 30 polypeptide separated by isoelectric focusing]
Abstract:
Variants of p 30 (iso-p 30s), the 30,000 dalton major polypeptide of murine C-type retraviruses, have been characterized in all virus strains by isoelectric focusing. Several of these iso-p 30s have been found to coexist in a given virus strain. In the present study, two iso-p 30s, characteristic of the Friend-Rauscher subgroup, separated by preparative isoelectric focusing of p 30 in thin layers of polydextran gel, were subjected to tryptic peptide mapping and aminoacid analysis. The two iso-p 30s, with isoelectric points (pI) of 6.5 and 7.1, were found to possess a partially different primary structure, with about 50% homology. The results are discussed.
Insights
Two variants of the major murine C-type retrovirus polypeptide p30, differing in isoelectric point, exhibit partial structural homology. This finding sheds light on the molecular diversity within retroviral proteins.
Area of Science:
- Virology
- Molecular Biology
- Protein Chemistry
Background:
- Murine C-type retroviruses possess a major 30,000 dalton polypeptide, p30.
- Isoelectric focusing has revealed multiple variants (iso-p30s) of this polypeptide within viral strains.
Purpose of the Study:
- To characterize the structural differences between two specific iso-p30 variants from the Friend-Rauscher subgroup.
- To determine the degree of primary structural homology between these variants.
Main Methods:
- Preparative isoelectric focusing in polydextran gel to isolate iso-p30s.
- Tryptic peptide mapping to analyze peptide fragments.
- Amino acid analysis to determine composition.
Main Results:
- Two iso-p30 variants with isoelectric points of 6.5 and 7.1 were isolated.
- These variants displayed a partially different primary structure.
- Approximately 50% homology was observed between the two iso-p30s.
Conclusions:
- The Friend-Rauscher subgroup of murine C-type retroviruses exhibits structural heterogeneity in its major p30 polypeptide.
- The identified iso-p30 variants possess distinct yet partially conserved primary structures, suggesting evolutionary or functional implications.