STUDIES ON THE RELATIONSHIP BETWEEN BACTERIAL BLOOD GROUP SUBSTANCE AND SOMATIC ANTIGEN BY MEANS OF ENZYMATIC ANALYSIS

Abstract

1. Non-reducing end in the determinant group of O antigen 5, related to FA activity of Salmonella paratyphi B, is considered a sugar similar to N-acetyl-D-galactosamine from the results of inhibition test by sugars in both systems - agglutination of erythrocytes adsorbed with a specific bacterial polysaccharide and precipitation against anti-5 serum. Non-reducing end in the determinant group of O antigen 40, involved in A activity of Salmonella riogrande, is also considered N-acetyl-D-galactosaminoyl-N-acetyl-D-glucosamine (?) from the results of inhibition test by sugars in the previous two systems using anti-40 serum, So far, however, has been Unsuccessful an attempt to destroy O antigen 5 and F_A activity of S. paratyphi B or O antigen 40 and A activity of S. riogrande by the enzyme preparation obtained from Clostridium tertium.
2. Non-reducing terminals in the determinant groups of an antigen identical with O antigen 43 of Salmonella and of B activity present in Escherichia coli O₈₆ are both assumed α-D-galactose from the results of inhibition test by sugars in agglutination of erythrocytes adsorbed with a specific bacterial polysaccharide and in precipitation against anti-43 serum. The enzyme preparation derived from Clostridium maebashi destroys B activity, without destroying the antigen identical with O antigen 43 in Salmonella, of E. coli O₈₆ to release galactose, galactosyl 1→3 or 1→6 galactose, galactosyl 1→4 galactose, galactosyl 1→4 galactosyl 1→4 galactose. Accordingly, the terminal determinant of the bacterial B activity is deduced to resemble exceedingly that of human water-soluble B substance, in connection with its linkage and configuration, but to be little different from O antigen 43.
3. Either of O antigen 13 and O(H) active substance of Salmonella poona is presumed to possess L-fucose in non-reducing end of these determinant groups from the results of inhibition test by sugars in agglutination of erythrocytes adsorbed with a specific polysaccharide and in precipitation against anti-13 serum. The enzyme preparation extracted from Bacillus fulminans causes to disappear completely O(H) activity as well as to decompose partly O antigen 13 of the bacteria to release large amounts of fucose and small amounts of hexose and N-acetylhexosamine as simple sugar. The enzyme preparation extracted from Bacillus cereus causes to vanish completely O(H) activity as well as to decompose better O antigen 13 than did the above-stated enzyme, to release relatively small amounts of fucose and hexose as simple sugar, and in addition, large amounts of oligosaccharides composed of glucose and galactose, or composed of one of the two, fucose, and hexosamine.