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Properties of contractile protein from bovine carotid artery

✍ Scribed by Mallin, Morton L.

Publisher
Wiley (John Wiley & Sons)
Year
1965
Tongue
English
Weight
447 KB
Volume
65
Category
Article
ISSN
0095-9898

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✦ Synopsis

A contractile protein was isolated from the cow carotid artery by extracting with a medium containing 0.6 M KCI. The enzymatic activity of the artery contractile protein resulted in the splitting of the terminal phosphate of ATP.2 The divalent metals Ca and Mg activated the enzyme with Ca showing the more pronounced activation. In addition to the studies on the ATP-ase activity other properties were investigated, such as viscosity, solubility in KC1 solutions, ATP-induced syneresis and sensitivity to relaxing factor. The properties of the contractile protein were those of actomyosin. The protein resembles uterine actomyosin with respect to its low ATPase activity and its viscosity values of 2 1 1 and ATP sensitivity.

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