Preparation and characterization of pig plasma and platelet gelsolins.
Pig plasma gelsolin has been prepared by a revised method involving poly(ethylene glycol) precipitation, chromatography on CM-cellulose and affinity chromatography on actin-Sepharose. Pig platelet gelsolin has been prepared by chromatography on DEAE-cellulose and actin-Sepharose. Partial chemical and proteolytic cleavage shows that the two proteins are closely related in their fragmentation patterns. The amino acid sequences are identical at the N-terminus of the platelet protein, but the plasma protein has an additional nine residues on the N-terminal side of the common sequence. Calcium binding studies show that the plasma protein has similar calcium binding properties to both macrophage and platelet gelsolins.
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D001792:Blood Platelets / Q000378:metabolism*; D002118:Calcium / Q000378:metabolism; D002135:Calcium-Binding Proteins / Q000097:blood*; D002384:Catalysis; D002845:Chromatography / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel; D019855:Ethylene Glycol; D005026:Ethylene Glycols; D018260:Gelsolin; D008840:Microfilament Proteins / Q000097:blood*; D010443:Peptide Chain Termination, Translational; D013552:Swine
D002135:Calcium-Binding Proteins; D005026:Ethylene Glycols; D018260:Gelsolin; D008840:Microfilament Proteins; D019855:Ethylene Glycol; D002118:Calcium