The crude supernatant of Lentinus edodes (L. edodes) was divided into two Cd-binding fractions, that is, Fraction I (Fr-I, MW>10, 000) and Fraction II (Fr-II, MW<10, 000) by gel filtration on Sephadex G-75. In the previous paper, we suggested that Fr-II contained a peptide with a molecular weight of about 700. In this paper, chemical forms of Cd in Fr-I were investigated. Fr-I was separated into 3 Cd-binding components, Fraction A (Fr-A, MW>450, 000), Fraction B (Fr-B, MW ca. 40, 000)and Fraction C (Fr-C, MW ca. 9, 000) by gel filtration on Sephadex G-150. Then, purification of Fr-A, Fr-B and Fr-C was performed by means of DEAE-cellulose, Sephadex G-150 and Sephadex G-25 column chromatography, respectively. Most of the Cd-containing components in Fr-A were eluted in Fraction A1 (Fr-A1, MW ca. 3, 500), those in Fr-B wereeluted in Fraction B1 (Fr-B1, MW ca. 3, 500) and Fraction B2 (Fr-B2, MW ca. 40, 000), and those in Fr-C were eluted in Fraction C1 (Fr-C1, MW ca. 3, 500). It was considered that the Cd-binding components, Fr-A1, Fr-B1 and Fr-C1, were identical and were dissociated from parent components to which each was bound as a conjugate or a weakly bonded complex. However, their chemical forms could not be determined. Another Cd-binding component, Fr-B2 was found to be a glycoprotein having high contents of acidic amino acids and saccharides.