title: Isolation and characterization of highly purified alpha-1-antitrypsin.
abstract: Highly purified human alpha-1-antitrypsin (phenotype MM) was obtained by an original method of preparative electrophoresis. The criteria of homogeneity were assured by one arc in crossed immunoelectrophoresis and one band on polyacrylamide gel. A unique N-terminal amino acid (pyroglutamic acid) and a unique C-terminal residue (lysine) were identified. Determined by gel electrophoresis, its molecular weight was 47,000 daltons.
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D006868:Hydrolysis; D007123:Immunoelectrophoresis, Two-Dimensional; D008239:Lysine / Q000032:analysis; D011761:Pyrrolidonecarboxylic Acid / Q000032:analysis; D000515:alpha 1-Antitrypsin / Q000032:analysis / Q000302:isolation & purification*
chemical_list: D000596:Amino Acids; D000515:alpha 1-Antitrypsin; D008239:Lysine; D011761:Pyrrolidonecarboxylic Acid