Comparative studies on the structures of the heat labile β-N-acetylhexosaminidases from human plasma and placenta

Abstract

1. 1. Human plasma and placenta β- N-acetylhexosaminidase A have been purified by a combination of salt precipitation, DEAE-cellulose, Concanavalin-Sepharose and Sephadex ehromatography. 2. 2. Comparative studies using rabbit antisera against plasma enzyme indicate similarity but not identity of the enzymes. Amino acid analyses before and after tyrpsin treatment of the enzymes confirm the immunological findings. 3. 3. Heat denaturation and circular dichroism studies also suggest structural similarity of the enzymes. 4. 4. Matrix analysis of circular dichroism data indicate that combinations of basis spectra, for α-helix, β-structure and random chain cannot fit the observed spectra of the enzymes.