All issues
Volume 28 (1973)
- Issue 6 Pages 489-
- Issue 5 Pages 401-
- Issue 4 Pages 357-
- Issue 3 Pages 315-
- Issue 2 Pages 213-
- Issue 1 Pages 22-
Volume 28, Issue 4
Displaying 1-4 of 4 articles from this issue
- |<
- <
- 1
- >
- >|
-
Yoshiki OGIHARA1973 Volume 28 Issue 4 Pages 357-366
Published: July 25, 1973
Released on J-STAGE: February 19, 2009
JOURNAL FREE ACCESSStudies were made to elucidate the mechanism of production of cytotoxic factor by sensitized lymphocytes in delayed-type allergy and the substantial entity of this factor in the chicken. Neonatally thymectomized or bursectomized chickens were immunized against Mycobacterium BCG, or human γ-globulin in Freund's complete adjuvant. The supernatants of cultures of sensitized splenic lymphocytes collected from them were examined for cytotoxic activities on chickembryo fibroblasts. The results obtained are as follows.
1) Delayed-type hypersensitivity was induced in bursaless birds having the T cell system but lacking the B cell system, but not in thymectomized birds lacking the T cell system. Cytotoxic factor began to be produced about 6 hours after the corresponding antigen had been added to the culture of sensitized lymphocytes. Then it was produced intensively for about 24 hours. Thereafter, its production was suppressed probably due to the presence of a feedback mechanism. It was also found that this factor exhibited “autotoxic” activity on sensitized lymphocytes themselves in the culture continually for more than 48 hours.
2) When sensitized lymphocytes were exposed to metabolic inhibitors, such as actinomycin D, puromycin, and 2, 4-dinitrophenol, the production of cytotoxic factor was markedly suppressed. This fact indicates that this factor is biosynthetized de novo in the sensitized lymphocytes and secreted into the extracellular medium.
3) Experiments were carried out by the fractionation of cytotoxic factor by gel-filtration with Sephadex G 200, DEAE-cellulose column chromatography of the culture supernatant, degradation with trypsin, and ultrafiltration by the Diaflo membrane of the cytotoxic fraction. From the results obtained, it was confirmed that the cytotoxic factor was a substance of protein nature contained in the α-globulin fraction, and had a molecular weight ranging from 50, 000 to 100, 000.
Discussion was made on the findings mentioned above in relation to some already known chemical mediators produced by sensitized mammalian lymphocytes, and on the biological significance of these findings in immune responses.View full abstractDownload PDF (1218K) -
Shigemi SATO, Suga TAHARA1973 Volume 28 Issue 4 Pages 367-374
Published: July 25, 1973
Released on J-STAGE: February 19, 2009
JOURNAL FREE ACCESSThe culture supernatants of Clostridium botulinum A, B, and F types (all proteolytic) contained two different enzymes. One of the enzymes had esterase activity against BAEE (α-N-benzoyl-arginine ethyl ester) and the other, proteinase activity against casein. Both enzymes were purified by the ammonium sulfate precipitation, DEAE-Sephadex chromatography, and gel filtration. These proteinases showed maximal activity at pH 9 against casein and were not inhibited by 1×10-3M DFP. These proteinases hydrolyzed di-and tripeptides, such as DL-alanylglycine, DL-alanylglycylglycine, DL-leucylglycine, and DL-leucylglycylglycine, but exclusive of glycylglycine and glycylglycylglycine. The molecular weights of the proteinases obtained from the 3 types were estimated to be about 25, 000 (A and B types) and 35, 000 (F type). The other properties and actions were the same among these enzymes. On the other hand, the purified esterases from the 3 types showed maximal activity at pH 7 against BAEE. The esterase activities were enhanced by the addition of 1×10-3M Ca++, Zn++, Mg++, and KCN. Cu++, cysteine, and PCMB reduced the esterase activity by 40-50%, but DFP did not. The molecular weight of esterase derived from each of the 3 types was estimated to be about 67, 000. The enzymes obtained from the 3 types had the same properties and actions.View full abstractDownload PDF (938K) -
1973 Volume 28 Issue 4 Pages 375-387
Published: July 25, 1973
Released on J-STAGE: February 19, 2009
JOURNAL FREE ACCESSDownload PDF (1635K) -
1973 Volume 28 Issue 4 Pages 389-391
Published: July 25, 1973
Released on J-STAGE: February 19, 2009
JOURNAL FREE ACCESSDownload PDF (295K)
- |<
- <
- 1
- >
- >|