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Mutarotase in erythrocytes: isolation and properties
Science (New York, N.Y.)
|October 27, 1967
Abstract:
Mutarotase was found in lysed human erythrocytes and in hemoglobin. The enzyme was partially purified by treatment with ethanol and chloroform at -15 degrees C. It was nondialyzable and heat sensitive, and was inhibited by D-galactose, L-arabinose, D-ribose, D-xylose, and D-arabinose.
Insights
Human erythrocytes contain mutarotase, an enzyme partially purified using ethanol and chloroform. This heat-sensitive enzyme
Area of Science:
- Biochemistry
- Enzymology
Background:
- Mutarotase activity was investigated in human red blood cells.
- The enzyme was detected within lysed erythrocytes and hemoglobin.
Purpose of the Study:
- To partially purify and characterize mutarotase from human erythrocytes.
- To identify factors affecting mutarotase activity.
Main Methods:
- Partial purification of mutarotase using ethanol and chloroform at low temperatures (-15°C).
- Assessment of enzyme properties including dialyzability and heat sensitivity.
- Testing the inhibitory effects of various sugars on enzyme activity.
Main Results:
- Mutarotase was successfully extracted from lysed human erythrocytes and hemoglobin.
- The enzyme was found to be nondialyzable and sensitive to heat.
- Several sugars, including D-galactose, L-arabinose, D-ribose, D-xylose, and D-arabinose, demonstrated inhibitory effects on mutarotase activity.
Conclusions:
- Human erythrocytes are a source of mutarotase.
- The enzyme exhibits characteristics of a heat-sensitive protein.
- Specific sugars can modulate mutarotase function, suggesting potential regulatory mechanisms.