Selective purification of cardiac myosin by a high-performance salicylate affinity column.
The cardiac muscle proteins, myosin and actin, were purified in one step using a salicylate-silica affinity column. The affinity columns were prepared by coupling sodium salicylate via its hydroxyl group to an Altex Ultraffinity-EP column. Crude detergent extracts from guinea pig hearts were passed through the column and the myosin-actin complex was then eluted with excess free salicylate or high salt. The affinity of cardiac myosin for immobilized salicylate was unique as myosin heavy chain from guinea pig leg muscle detergent extracts could not be purified by this procedure. Commercially purified rabbit leg muscle myosin also appeared to have no interaction with the salicylate affinity column, suggesting that the column is specific for cardiac myosin.
Strohsacker
M W
MW
Department of Molecular Pharmacology, Smith Kline & French Laboratories, King of Prussia, PA 19406-0937.
Minnich
M D
MD
Clark
M A
MA
Shorr
R G
RG
Crooke
S T
ST
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D006168:Guinea Pigs; D009206:Myocardium / Q000032:analysis*; D009218:Myosins / Q000302:isolation & purification*; D012459:Salicylates; D012967:Sodium Dodecyl Sulfate; D013056:Spectrophotometry, Ultraviolet
D000596:Amino Acids; D012459:Salicylates; D012967:Sodium Dodecyl Sulfate; D009218:Myosins