Dynamic affinity chromatography of heavy meromyosin subfragment-1

Avraham Oplatka*, Raphael Lamed, Andras Muhlrad

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

Heavy meromyosin subfragment-1 and its trinitrophenylated derivative 3ave been chromatographed on immobilized ATP, ADP and adenosine 5′-(β,γ-imino)triphosphate affinity chromatography columns, in the presence and in the absence of Mg2+ or Ca2+. Splitting of bound ATP was followed by using [γ-3 2P]ATP columns. While the divalent cations had little effect on the chromatographic pattern in the case of the non-hydrolyzable ADP and adenosine 5′(β,γ-imino)triphosphate, they catalyzed splitting in the case of ATP and at the same time strongly increased the affinity of adsorption of the proteins. The protein-elution and the Pi-release patterns were different for the native and the modified proteins. These results have been interpreted in terms of protein binding to the various intermediates of the ATP hydrolysis reaction.

Original languageEnglish
Pages (from-to)20-27
Number of pages8
JournalBiochimica et Biophysica Acta - General Subjects
Volume385
Issue number1
DOIs
StatePublished - 14 Mar 1975
Externally publishedYes

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