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Comparison between prochymosin and pepsinogen from lamb and calf
M Baudys1, T G Erdene, V Kostka
1Department of Biochemistry, Czechoslovak Academy of Sciences, Prague.
Summary
Mongolian lamb prochymosin and pepsinogen A were purified and found to be glycosylated. These enzymes show close relationships with cattle counterparts, indicating conserved proteinase structures.
Area of Science:
- Biochemistry
- Proteomics
- Comparative analysis of animal proteinases
Background:
- Prochymosin and pepsinogen A are key digestive enzymes.
- Understanding variations across species aids in comprehending enzyme evolution and function.
- Mongolian lamb (Ovis platyurea) serves as a model for studying these proteinases.
Purpose of the Study:
- To purify prochymosin and pepsinogen A from Mongolian lamb.
- To characterize these enzymes and compare them with homologous proteins from other species.
- To investigate the glycosylation status of lamb proteinases.
Main Methods:
- Homogeneous purification using salt precipitation, gel filtration, and ion-exchange chromatography.
- Immunoelectrophoresis for immunochemical identity assessment.
- N-terminal amino acid sequencing and amino acid composition analysis.
Main Results:
- Prochymosin and pepsinogen A were successfully purified to homogeneity.
- Partial immunochemical identity was observed between lamb and cattle chymosins and pepsins.
- Sequence and composition data confirmed a close relationship between lamb and cattle proteinases.
- Both lamb prochymosin and pepsinogen A were identified as glycosylated.
Conclusions:
- Lamb prochymosin and pepsinogen A share structural and functional similarities with their cattle counterparts.
- The glycosylation of these enzymes in lamb suggests conserved post-translational modifications.
- This study provides insights into the evolutionary conservation of aspartic proteinases in ruminants.