Serologic dissection of HLA-D specificities by the use of monoclonal antibodies

To study the gene products of the HLA complex, we produced two monoclonal antibodies, termed HU-18 and HU-23. They were active in complement-dependent cytotoxicity and detected B-cell alloantigens encoded by a locus (or loci) linked to HLA. When three types of HLA-DR4 homozygous B-cell lines with different HLA-D specificities were tested for reactivity with HU-18 and HU-23, they displayed distinct reaction patterns depending on the HLA-D specificities they possessed: EBV-Wa (HLA-DYT homozygous), negative for both HU-18 and HU-23; KT2 and KOB (HLA-DKT2 homozygous), positive only for HU-18; and ER (HLA-Dw4 homozygous), positive for both. These differential reaction patterns were further confirmed by testing against a panel of 17 HLA-DR4-positive peripheral blood lymphocytes with known HLA-D specificities. Thus, these monoclonal antibodies allow us to identify HLA-DYT, HLA-DKT2, and HLA-Dw4 solely by serologic methods. This is the first clearcut serologic identification of these three HLA-DR4-associated HLA-D specificities, which have been indistinguishable by conventional serology and identified only by cellular techniques. It is hoped that immunochemical investigations using HU-18 and HU-23 will advance our understanding of the HLA-D region on a molecular level.     

MUCOPOLYSACCHARIDES PRODUCED BY A STRAIN OF CLOSTRIDIUM PERFRINGENS.

Izumi, Kunihiko (Kanazawa University, Kanazawa, Japan). Mucopolysaccharides produced by a strain of Clostridium perfringens. J. Bacteriol. 83:956-959. 1962.-A new series of mucopolysaccharides was isolated from the culture medium of Clostridium perfringens and partially purified by the use of a column of anion-exchange resin. A large part of the substance was composed of neutral sugars, amino sugars, uronic acids, and oligopeptides, suggesting a structure analogous to that of bacterial cell walls. Acidic amino acids, especially aspartic acid, were the main constituents of the oligopeptides. The substance exhibited high viscosity when dissolved in water. The degree of viscosity in each fraction seemed to depend on the content of amino sugars and the chain length of the oligopeptides.     

Active Oxygen Contributes to the Major Part of Chromosomal Aberrations in V79 Chinese Hamster Cells Exposed to N-Hydroxy-2-Naphthylamine

N-hydroxy-2-naphthylamine (NOH-2NA). an active metabolite of human occupational bladder carcinogens, induced, in V79 Chinese hamster cells. chromosomal aberrations which were suppressed in the presence of catalase and/or superoxide dismutase. The induction of the aberrations was more efficient in a more basic pH in parallel with the generation of hydrogen peroxide from NOH-2NA. The possible role of the oxidation product of NOH-2NA in the induction of the aberrations is discussed.     

Xenobrama microlepis,a new genus and species of bramid fish,from subantarctic waters of the South Pacific

Xenobrama microlepis gen. et sp. nov. is described on the basis of 17 adult and subadult specimens collected by surface gill nets, bottom trawl and midwater trawl from the subantarctic waters of the South Pacific Ocean. This monotypic new genus is distinguished from other bramid genera by the following characters: inner lower edges of mandible touching each other (except near symphysis); gill rakers short, thick, and stout; subpectoral region very narrow; interpelvic space flat and wide; vertebrae 49–51; and scales in longitudinal series more than 83. The new taxon is widely distributed in the high seas of the South Pacific, 38–54°S, 79–176°W, but is rather rare compared toBrama spp. in catches of drift gill nets.     

Construction of a chimeric series of Bacillus cyclomaltodextrin glucanotransferases and analysis of the thermal stabilities and pH optima of the enzymes

The cyclomaltodextrin glucanotransferase (CGTase, EC 2.4.1.19) gene from the alkalophilic Bacillus sp. strain no. 17-1 was cloned in Escherichia coli. The cloned CGTase gene consisted of a single open reading frame which would encode a polypeptide of 713 amino acids, and the first 27 amino acid residues comprised a signal peptide. The nucleotide sequence and the amino acid sequence of this CGTase (CGTase 17-1) gene had strong homology with those of the CGTase (CGTase 38-2) gene previously cloned in our laboratory from the alkalophilic Bacillus sp. strain no. 38-2, although the enzymic properties of the CGTase 17-1 were distinct from those of the CGTase 38-2. To analyse those enzymic properties further, we constructed 12 chimeric CGTases using three restriction nuclease sites and compared the enzymic properties of the chimeric CGTases. The N-terminal part of the enzyme was important for heat stability, and the pH-activity profile was influenced by both the N- and the C-terminal parts. A third segment was less important for enzymic properties.