Shoei Iseki

Immunochemical Studies on Blood Group H and B Substances from Human Hair

SummaryBlood group H and B substances were extracted from urea-treated human hair of group O and B individuals, respectively, with methanol-ethyl ether (1:1,v/v) and chloroform-methanol (1:1,v/v). The blood group activities of H and B substances were destroyed by H-decomposing enzyme (α-l-fucosidase) fromBacillus fulminans and B-decomposing enzyme (α-d-galactosidase) fromClostridium sporogenes Maebashi, respectively. It is concluded therefore that the extract from the hair of group O contained blood group H-active glycolipid with α-l-fucose as the non-reducing sugar and the one from group B contained blood group B-active glycolipid with α-d-galactose as the non-reducing sugar.ZusammenfassungDas H-blutgruppenaktive Glycolipoid wurde mit Methanoläther (1:1,v/v) und Chloroform-Methanol (1:1,v/v) aus Harnstoff-behandelten Haaren extrahiert. Wenn nach Behandlung der H-Substanz von Haaren mit H-zerstörenden Enzym (a-l-Fucosidase) ausBacillus fulminans H-Aktivität spurlos verschwindet, so kann es sein, daß α-l-Fucose für die H-Aktivität von Haarglycolipoid benötigt wird. Das B-blutgruppenaktive Glycolipoid wurde aus Menschenhaaren extrahiert. Durch Einwirkung von B-zerstörendem Enzym (α-d-Galaktosidase) ausClostridium sporogenes Maebashi auf das B-Glycolipoid aus Haaren, kommt nunmehr die H-Eigenschaft nach Inaktivierung von B zum Vorschein. Darum kann es sein, daß α-d-Glaktose für die B-Aktivität vom Haarglycolipoid benötigt wird.

SOME IMMUNOCHEMICAL PROPERTIES OF Lea -AND Leb-ACTIVE SUBSTANCES IN HUMAN URINE

Lea‐ and Leb‐active substances present in normal human urine were isolated by sequential membrane filtration, column chromatography with DEAE‐Sephadex (A‐25), and gel filtration of Bio‐Gel (P‐6). Lea‐active substance with the highest activity was obtained in the P‐1 fraction (0.8 mg/1) from urine of a non‐secretor type by the final gel filtration. Leb‐active substance with the highest activity was also obtained in the P‐1 fraction (0.2 mg/1) from urine of a secretor type. The P‐1 of the non‐secretor inhibited Lea‐anti‐Lea haemagglutination minimally at 4 μg/ml, and the P‐1 of the secretor inhibited Leb‐anti‐Leb haemagglutination at 1 μg/ml. Both P‐1 fractions possessing Lea or Leb activity were characteristic in having a much higher fucose content than other isolated fractions, and seemed to be complex carbohydrates with molecular weights of the order of 4–5 × 103.

GENETIC RECOMBINATION BETWEEN ESCHERICHIA COLI K‐12 AND E. COLI STRAINS WITH BLOOD GROUP‐ACTIVE ANTIGENS

The genetic determinants responsible for the specificities of somatic antigens of Escherichia coli 2B‐V, O6 and O86, which also have blood group H, A and B activity, respectively, are located near the his locus on chromosomes.