Preparation of highly active (Na + + K +)-ATPase from the outer medulla of rabbit kidney

It is described how (Na + + K +)-ATPase from the outer medulla of rabbit kidney was purified to a specific activity of 881 ± 25 moles Pi/mg protein per hr at 37 C. The procedure consists of treatment of a microsomal fraction with deoxycholate and subsequent fractionation by differential centrifugati...

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Bibliographic Details
Published inBiochemical and biophysical research communications Vol. 37; no. 1; pp. 39 - 46
Main Authors Leth Jørgensen, P., Skou, J.C.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.01.1969
Subjects
Adenosine Triphosphatases - isolation & purification
Animals
Bile Acids and Salts
Centrifugation, Density Gradient
Chemical Phenomena
Chemistry
Enzyme Activation
Kidney - enzymology
Magnesium
Methods
Microsomes - enzymology
Ouabain
Potassium
Rabbits
Sodium
Ultracentrifugation
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Summary:It is described how (Na + + K +)-ATPase from the outer medulla of rabbit kidney was purified to a specific activity of 881 ± 25 moles Pi/mg protein per hr at 37 C. The procedure consists of treatment of a microsomal fraction with deoxycholate and subsequent fractionation by differential centrifugation and sucrose gradient centrifugation. The “purity” of the preparation was estimated to be 31–61%.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(69)90877-8