PubMed Health⌕ Search

Biomedical subjects

K ONOUE

Publications and source records attributed to K ONOUE.

11 recordsLinked to original sources
PubMed1964

ANTIGEN-BINDING ACTIVITY OF 6S SUBUNITS OF BETA-2-MACROGLOBULIN ANTIBODY.

Direct evidence is provided for the antigen binding activity of the 6S subunits formed by reduction and alkylation of rabbit beta2-macroglobulin antibody. Binding activity of the subunits was clearly demonstrated by radioimmunoelectrophoresis with a preparation of purified rabbit antibody against the p-azobenzenearsonate group, which contained 40 percent of beta2M-antibody. The precipitate arc formed between the subunits and sheep antiserum against rabbit macroglobulin was shown to bind radioactive antigen specifically.

Animals↗
PubMed1963

CHEMICAL STUDIES ON CELLULAR COMPONENTS OF BORDETELLA PERTUSSIS. III. ISOLATION OF HIGHLY POTENT TOXIN FROM BORDETELLA PERTUSSIS.

Onoue, Kaoru (Kyushu University, Fukuoka, Japan), Masayasu Kitagawa, and Yuichi Yamamura. Chemical studies on cellular components of Bordetella pertussis. III. Isolation of highly potent toxin from Bordetella pertussis. J. Bacteriol. 86:648-655. 1963.-The thermolabile toxin of Bordetella pertussis was extracted at alkaline pH with 0.15 m saline from the disrupted cells. The toxin was purified successively by calcium phosphate gel treatment, ammonium sulfate fractionation, precipitation with potassium phosphate at alkaline pH, and finally by chromatography on a diethylaminoethyl cellulose column. Although the purified toxin still contained a small amount of agglutinin-absorbing activity, and inhomogeneity was detected by the agar gel diffusion test, the lethal and skin-necrotizing activities were much higher than those previously reported. The data obtained suggest that the toxin is proteinaceous.

Agglutinins↗
PubMed1961

Chemical studies on cellular components of Bordetella pertussis. I. Purification and properties of agglutinogen.

Onoue, Kaoru, (Kyushu University, Fukuoka, Japan), Masayasu Kitagawa, and Yuichi Yamamura. Chemical studies on cellular components of Bordetella pertussis. I. Purification and properties of agglutinogen. J. Bacteriol. 82:648-656. 1961.-A method is described for the preparation of the agglutinogen of Hemophilus pertussis in phase I by methanol precipitation and ion-exchange chromatography. High homogeneity of this agglutinogen was evidenced by chromatography, but a trace of impurity was detected by ultracentrifugal analysis and by an agar gel diffusion test.The agglutinogen produced an allergic skin reaction in rabbits which had been immunized with whole phase I organisms. Chemical studies indicate that the agglutinogen should be a simple protein in nature. The approximate molecular weight was determined to be 10,000 by Archibald's method.

Animals↗