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Published on: May 4, 2013
F1-ATPase of Micrococcus lysodeikticus is not a glycoprotein
Biochimica Et Biophysica Acta
|December 14, 1981
Summary
The F1-ATPase enzyme from Micrococcus lysodeikticus is not a glycoprotein. Carbohydrate presence is due to lipomannan contamination, not covalent linkage to the enzyme.
Area of Science:
- Biochemistry
- Molecular Biology
- Enzymology
Background:
- Previous studies suggested Micrococcus lysodeikticus F1-ATPase is a glycoprotein containing mannose and glucose.
- Purified F1-ATPase preparations showed significant carbohydrate content (2.7-10.8%).
Purpose of the Study:
- To investigate the alleged glycoprotein nature of M. lysodeikticus F1-ATPase.
- To determine if carbohydrates are covalently linked to the F1-ATPase enzyme.
Main Methods:
- Extensive purification of F1-ATPase using DEAE-Sephadex A25 chromatography.
- Separation of concanavalin A-reactive components using immunoelectrophoresis and concanavalin A-Sepharose 4B chromatography.
- Analysis of sugar content by gas-liquid chromatography and subunit profiles by SDS-PAGE.
Main Results:
- Concanavalin A-reactive components, identified as lipomannan, were separated from the ATPase.
- Concanavalin A-Sepharose 4B chromatography removed all detectable mannose without affecting ATPase activity.
- No changes in subunit composition were observed after carbohydrate removal.
Conclusions:
- The F1-ATPase of M. lysodeikticus is not a glycoprotein.
- The detected carbohydrates are attributed to contamination with lipomannan, not covalent linkage to the enzyme.
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