Identification of calcium binding proteins from brain.
A procedure was worked out for purification and identification of calcium-binding proteins from bovine brain using Ca2+-dependent, reversible binding to a hydrophobic support, phenyl-Sepharose, as the method of isolation. These proteins could be visualized during and after their separation by running them on non-denaturing polyacrylamide gels, blotting to Zeta-probe paper, and autoradiographing with 45Ca2+. About 24 polypeptides could be seen in this fraction on SDS (Laemmli) gels and about 8-10 native, Ca2+-binding proteins could be seen on non-denaturing gels and on blots of their 45Ca2+ autoradiographs. Some of these proteins could be purified further by chromatography on DEAE-Sephacel and still retain their 45Ca2+-binding activity.
Moore
B W
BW
Washington University School of Medicine, Department of Psychiatry, St. Louis, Mo 63110.
D000818:Animals; D001923:Brain Chemistry; D002135:Calcium-Binding Proteins / Q000302:isolation & purification*; D002417:Cattle; D013347:Subcellular Fractions / Q000032:analysis
D002135:Calcium-Binding Proteins