Isolation and physico-chemical properties of blood platelet alpha-actinin.
A procedure for the isolation of alpha-actinin from human blood platelets is described. Typical yields were 10-13 mg from 48 g of frozen platelets. The purified platelet alpha-actinin has many physico-chemical properties (molecular weight in native state, molecular weight in denaturing conditions, Stokes radius, ellipticities at 208 and 221 nm) similar to those of muscle alpha-actinins. However, in contrast to muscle alpha-actinins, it is composed of isoforms containing subunits of slightly different molecular weights and its effect on actin gelation is calcium-sensitive. These two characteristics are common to other known non-muscle alpha-actinins.
D000185:Actinin / Q000097:blood* / Q000302:isolation & purification; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001792:Blood Platelets / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D005895:Gizzard, Avian / Q000032:analysis; D006801:Humans; D008970:Molecular Weight; D009124:Muscle Proteins / Q000097:blood*; D009132:Muscles / Q000032:analysis; D013552:Swine; D014422:Turkeys
D000596:Amino Acids; D009124:Muscle Proteins; D000185:Actinin