Abstract
A method is described for purification of P6, MRP8, and MRP14, three calcium-binding proteins assigned to the S100 protein family. The purification procedure included preparation of human granulocytes, ammonium sulfate precipitation, and anion-exchange chromatography and resulted in the copurification of P6, MRP8, and MRP14. Individual proteins were separated by either preparative isoelectric focusing or preparative SDS-PAGE. The procedure was carried out in the course of 4 days and yielded several milligrams of essentially pure P6, MRP8, and MRP14 in either native or denatured form.
Copyright 1998 Academic Press.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Sequence
-
Antigens, Differentiation / blood
-
Antigens, Differentiation / chemistry
-
Antigens, Differentiation / isolation & purification*
-
Calcium-Binding Proteins / blood
-
Calcium-Binding Proteins / chemistry
-
Calcium-Binding Proteins / isolation & purification*
-
Calgranulin A
-
Calgranulin B
-
Cells, Cultured
-
Chromatography, Ion Exchange
-
Electrophoresis, Polyacrylamide Gel
-
Granulocytes / metabolism*
-
Humans
-
Isoelectric Focusing
-
Molecular Sequence Data
-
S100 Proteins*
Substances
-
Antigens, Differentiation
-
Calcium-Binding Proteins
-
Calgranulin A
-
Calgranulin B
-
S100 Proteins
-
calcium-binding protein p6, human