Immunological similarity between fractions

To elucidate some enzymatic characteristics of the isolated laccases I, II, and III, substrate specificities for several simple phenols, electrophoresis patterns, ultraviolet spectra, electron spin resonance spectra, copper content, and immunological similarities were investigated. Tyrosine, tannic acid, g c acid, hydroquinone, catechol, pyrogallol, p-cresol, homocatechol, a-naphthol, -naphthol, p-phenylenediamine, and p-benzoquinone as substrates. No differences in the specificities of these substrates was found. The UV spectra for the laccases under stucfy are shown in Figure 4. Laccase III displays three adsorption bands (280, 405, and 600nm), laccase II shows one band 280nm), and laccase I shows two bands (280 and 405 nm). These data appear to indicate differences in chemical structure. The results of the copper content analysis (10) and two-dimensional electrophoresis also indicate that these fractions are completely different proteins (10), Therefore, we may expect differences in substrate specificities between the three laccase fractions for more lignin-like substrates, yet no difference for some simple phenolic substrates. 

The peptide moiety of wax D fractions of human strains seems to be necessary for the activity of these fractions as immunological adjuvants (see p. 235) this may be due to the close chemical similarity between the structure of the water-soluble portion of wax D and the cell wall of Mycobacteria, since the latter contains the same three amino acids (alanine, glutamic acid, and a, c-diaminopimelic acid) and the same sugars (arabinose, mannose, galactose, and aminohexoses). Wax D of human strains might be considered to be a monomer of the cell wall, heavily esterified with mycolic acid. 

---