A Saito, H Sinohara
Index: Biochem. Mol. Biol. Int. 46(1) , 27-34, (1998)
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Amino acid sequencing of the ficin-derived C-terminal fragments of alpha-1-antiproteinase (also called alpha-1-antitrypsin or alpha-1-proteinase inhibitor) prepared from rabbit plasma revealed the presence of the E isoform, which had been confirmed in the cDNA library in addition to the F and S-1 forms. The S-2 form was identified in inflamed rabbit plasma. The ficin digest of human plasma alpha-1-antitrypsin resulted in a major fragment of the M type. Multiple forms of alpha-1-antiproteinase in the rabbit plasma implicate the unknown functions other than the inhibition of neutrophil elastase.
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