A simple procedure for the preparation of highly purified (sodium + potassium) adenosinetriphosphatase from the rectal salt gland of Squalus acanthias and the electric organ of Electrophorus electrieus
✍ Scribed by John F. Dixon; Lowell E. Hokin
- Publisher
- Elsevier Science
- Year
- 1978
- Tongue
- English
- Weight
- 641 KB
- Volume
- 86
- Category
- Article
- ISSN
- 0003-2697
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✦ Synopsis
A simple purification procedure for the Na,K-ATPase from membranes of the rectal gland of Squalus acanthias or crude microsomal fractions from the electric organ of Hectrophorus electricus is presented here. The purification procedure consists of solubilization of the Na,K-ATPase with the nonionic detergent, Lubrol WX, chromatography of the diluted Lubrol extract on aminoethyl cellulose, and ammonium sulfate fractionation (1) of the concentrated eluate from the aminoethyl cellulose column. The yields of final purified enzyme are comparable to the earlier purification (l-4) involving the expensive and cumbersome zonal centrifugation step. The purity of the final enzyme. as attested to by specific activity and sodium dodecyl sulfate-polyacrylamide gel electrophoresis, is as great or greater than that previously reported for the enzyme purified by the procedure involving zonal centrifugation. The simplicity of the present procedure, coupled with the ready commercial availability of electric eels which are quite hardy on shipment. makes purification of the Na,K-ATPase widely available to workers in the field.