Proteolytic cleavages in alpha 1-antitrypsin and microheterogeneity.
Antitrypsin was resolved into two pools by ion-exchange chromatography. Pool 2 contained three anodal isoinhibitors and an N-terminal sequence identical with the one found by others. Pool 1 contained, in addition to the anodal ones two cathodal isoinhibitors as well. The sequencing data of Pool 1 indicate that the cathodal proteins are formed from the anodals by a cleavage of the Gly5-Asp6 bond in the molecule.
D000595:Amino Acid Sequence; D002852:Chromatography, Ion Exchange; D006801:Humans; D007525:Isoelectric Focusing; D000515:alpha 1-Antitrypsin / Q000032:analysis*
D000515:alpha 1-Antitrypsin