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Preparation and characterization of an enzymatically active immobilized derivative of myosin

Biochimica Et Biophysica Acta

Nov 20, 1975

E S ElgartM D Rosenberg

PMID: 72

Abstract

Purified skeletal muscle myosin (EC 3.6.1.3) has been covalently bound to Sepharose 4B by the cyanogen bromide procedure. The resulting complex, Sepharose-Myosin, possesses adenosine triphosphatase activity and is relatively stable for long periods of time. Under optimal binding conditi...read more

Mentioned in this Paper

Calcium
Adenosine Triphosphatases
N-Actin
Plasma Protein Binding Capacity
Lysine
Bromides Measurement
Cations
Slow-K
Polymers
Hydrolase
1
Paper Details
References

Preparation and characterization of an enzymatically active immobilized derivative of myosin

Biochimica Et Biophysica Acta

Nov 20, 1975

E S ElgartM D Rosenberg

PMID: 72

DOI:

Abstract

Purified skeletal muscle myosin (EC 3.6.1.3) has been covalently bound to Sepharose 4B by the cyanogen bromide procedure. The resulting complex, Sepharose-Myosin, possesses adenosine triphosphatase activity and is relatively stable for long periods of time. Under optimal binding conditi...read more

Mentioned in this Paper

Calcium
Adenosine Triphosphatases
N-Actin
Plasma Protein Binding Capacity
Lysine
Bromides Measurement
Cations
Slow-K
Polymers
Hydrolase
1

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