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J. Biochem, 1987, Vol. 101, No. 4 987-995
© 1987 Japanese Biochemical Society


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Further Characterization and Structural Studies on Human Placenta Lectin1

Jun HIRABAYASHI*, Hiroshi KAWASAKI**, Koichi SUZUKI** and Ken-ichi KASAI*

*Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Teikyo University Sagamiko, Kanagawa 199–01;
**Department of Biology, The Tokyo Metropolitan Institute of Medical Science Bunkyo-ku, Tokyo 113

The properties of a previously purified ß-galactoside-binding lectin of human pla-centa were studied in detail. Isoelectric focusing gave multiple bands around pH 4.9, although the lectin preparation was homogenous in SDS-polyacrylamide gel electrophoresis. High-performance gel chromatography suggested that the lectin exists mainly as the monomer and that a small fraction forms a dimer. From all the criteria examined, human placenta lectin resembles one of the chick lectins obtained from embryonic skin or adult intestine (subunit molecular weight: 14, 000). The lectin was inactivated by thiol-modifying reagents, p-chloromercuribenzoic acid and N-ethylmaleimide. Reduced and carboxymethylated lectin contained five carboxymethylated cysteines per subunit, and five free thiol groups were titrated by using 5, 5'-dithio-bis(2-nitrobenzoic acid) Preliminary sequence analysis showed the presence of a region highly homologous to the corresponding region of the chick lectin (13 identical residues out of 18 from number 70 to 87 of the chick lectin), suggesting a close evolutionary relation between these lectins and the importance of this conserved region in the function of the lectins.

1This study was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.


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