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The membrane relationship of microsomal nucleoside diphosphatase
The International Journal of Biochemistry
|January 1, 1982
Summary
Agents altering microsomal nucleoside diphosphatase (NDPase) activity were investigated. Trypsin and toluene activated NDPase, with toluene facilitating protein release from microsomes, shedding light on NDPase-membrane interactions.
Area of Science:
- Biochemistry
- Cell Biology
- Enzymology
Background:
- Microsomal nucleoside diphosphatase (NDPase) plays a role in cellular processes.
- Understanding the regulation of NDPase activity and its interaction with cellular membranes is crucial.
Purpose of the Study:
- To investigate the effects of agents that modify microsomal NDPase activity and sedimentability.
- To elucidate the mechanisms by which NDPase interacts with microsomal membranes.
Main Methods:
- Enzyme activity assays to measure NDPase function.
- Electrophoresis to analyze protein composition and integrity.
- Proteolytic digestion under anaerobic conditions to assess enzyme protection.
Main Results:
- Trypsin activated NDPase, likely by stimulating endogenous lipid peroxidation.
- Toluene also activated NDPase, with the enzyme remaining in a particulate fraction.
- Eighty percent of vesicular NDPase was protected from anaerobic proteolytic degradation.
- NDPase and other proteins were readily released from microsomes following toluene treatment.
Conclusions:
- NDPase activity can be modulated by specific agents.
- The interaction between NDPase and the microsomal membrane influences its susceptibility to proteolysis.
- Toluene treatment offers a method for releasing NDPase and associated proteins from microsomes.