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Volume 26 (1982)
- Issue 6 Pages 411-
- Issue 5 Pages 333-
- Issue 4 Pages 259-
- Issue 3 Pages 159-
- Issue 2 Pages 71-
- Issue 1 Pages 1-
Volume 26, Issue 5
Displaying 1-11 of 11 articles from this issue
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Sadao Kobayashi1982 Volume 26 Issue 5 Pages 333-334
Published: October 25, 1982
Released on J-STAGE: March 31, 2009
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Kazuo Shimao1982 Volume 26 Issue 5 Pages 335-339
Published: October 25, 1982
Released on J-STAGE: March 31, 2009
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Tatsumi Baba, Miwa Baba, Hiroko Tohge, Mitsuko Ichimura1982 Volume 26 Issue 5 Pages 341-346
Published: October 25, 1982
Released on J-STAGE: March 31, 2009
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Morimichi Fukuda, Shoji Yamada1982 Volume 26 Issue 5 Pages 347-355
Published: October 25, 1982
Released on J-STAGE: March 31, 2009
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Kiyoko Sano, Hiroko Cho, Akihiko Shiba, Makoto Nakao1982 Volume 26 Issue 5 Pages 357-362
Published: October 25, 1982
Released on J-STAGE: March 31, 2009
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Tsuyoki Kadofuku, Takashi Manabe, Tsuneo Sato, Tsuneo Okuyama1982 Volume 26 Issue 5 Pages 363-369
Published: October 25, 1982
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSWe used fluorescein isothiocyanate (FITC) as a stain for the detection of two-dimensionally separated proteins. Human serum proteins were pre-labeled with FITC by mixing serum and a FITC solution at 0°C and pH 9.2 for 24 hours and subjected to two-dimensional electrophoresis in the absence of denaturing agents. The distribution of labeled proteins on the slab gel could be observed during and just after the electrophoretic run by irradiation with UV light.
When the FITC concentration was below 3.5mM in serum-FITC mixture, the mobilities of serum proteins did not differ from those of the native proteins. By controlling the FITC concentration, selective labeling of specific serum proteins was possibleView full abstractDownload PDF (6439K) -
Satoshi Unakami, Tomoko Hirama, Yoshifumi Tanimoto1982 Volume 26 Issue 5 Pages 371-377
Published: October 25, 1982
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSThe biochemical properties of creatine kinase (CK) isoenzymes were compared in various animals and the following characteristics were noted. 1. Isoenzyme electrophoretic patterns with CK1 and CK3 were observed in rat, rabbit, dog, miniature pig, mouse, and monkey plasma. 2. The activity of platelet rich plasma CK was much higher than that of the corresponding platelet poor plasma enzyme in rabbit, dog, rat, and miniature pig. 3. Plasma CK was markedly different in substrate affinity among the species. The apparent Km values well correlated with the percentage of CK1 or CK3 fraction in the plasma of various animals. 4. Upon incubation at 37°C, CK activities in rat and mouse plasma decreased rapidly, and the recovery of enzyme activities was only slight after the addition of sulfhydryl agents. On the other hand, in the presence of sulfhydryl agents, CK in human and monkey plasma were completely protected from loss of activity at 37°C.View full abstractDownload PDF (1806K) -
Masaki Inoue, Tetsuro Shono, Shunichi Koga, Hiroshi Ibayashi1982 Volume 26 Issue 5 Pages 379-383
Published: October 25, 1982
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSWe established a simple method for measuring HDL subfraction cholesterols by gradient polyacrylamide gel electrophoresis (gradient PAGE). Prestained human serum was separated into two major bands identical with HDL2 and HDL3 by the gradient PAGE. HDL-cholesterol (HDL-C) obtained by precipitation method was divided according to HDL2/HDL3 ratio determined by densitometry of the electrophoretic pattern. HDL subfraction cholesterols determined by this method was well correlated with those measured by zonal ultracentrifugation (HDL2-C: r=0.98, HDL3-C: r=0.94, n=11). Mean serum HDL2-C level was significantly higher in normal females than in normal males (p<0.01). HDL3-C levels were significantly decreased in liver diseases, especially in cirrhotics. This simple electrophoretic method for quantification of HDL2 and HDL3 is suitable for clinical application in various pathological states.View full abstractDownload PDF (1834K) -
Takehiro Kadowaki, Mitsutaka Yoshida, Zensho Inafuku, Tutomu Takata1982 Volume 26 Issue 5 Pages 385-391
Published: October 25, 1982
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSLactate dehydrogenase† (LDH) activity and LDH isozyme in seven tissues of ddn strain mice during development from the embryo to the adult were investigated. The following results were obtained: (1) Comparison of the LDH activities in the various tissues on the 19th day of gestation and the 7th day after birth showed that the activities in the kidneys, liver and skeletal muscle increased, while, those in the cerebrum, cerebellum, heart and lungs decreased on the 7th day after birth. (2) The main isozyme activity on the 7th day after birth shifted to LDH-4 in the cerebrum and to LDH-3 in the cerebellum and heart. (3) Tissue specific isozyme pattern was seen in the cerebrum on the 56th day after birth and the isozyme activities were in the following order: LDH-3>LDH-1>LDH-4>LDH-2…. In the cerebellum, the pattern was seen on the 21st day after birth with a gradual decrease of isozyme activity from LDH-1 to LDH-5. In the lungs, the isozyme activities were LDH-5>LDH-4… from the 12th day of gestation and even after birth.View full abstractDownload PDF (654K) -
Takayoshi Matsuo, Seiichi Suzuki, Izumi Sakakibara, Hiroshi Amemiya1982 Volume 26 Issue 5 Pages 393-396
Published: October 25, 1982
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSα1-Antitrypsin (α1-AT) was isolated from normal human plasma by the method described by Pannel et al. Effect of isolated α1-AT treatment of lymphocytes on the immune response of normal human peripheral blood lymphocytes was studies by plaque-forming cells assay using protein-A coated neuraminidase treated goat erythrocyte. α1-AT was found to have suppressive effect on immunoglobulin production of normal human peripheral blood lymphocyte stimulated with pokeweed mitogen. The suppressive effect of α1-AT treated B cell was stronger than that of α1-AT treated T cell.View full abstractDownload PDF (399K) -
Kiyoko Sano, Hiroko Cho, Akihiko Shiba, Makoto Nakao1982 Volume 26 Issue 5 Pages 397-402
Published: October 25, 1982
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSAnalysis of serum γ-GTP isoenzymes was attempted with isoelectric focusing using agarose gel as a supporting medium. After testing various conditions to obtain electrophoretic patterns with good reproducibility, suspension of Ampholine in Agarose IEF was finally chosen as a supporting medium, and electrolysis at 6.25W/plate (length 12.5cm×width 11cm) for 1hr under cooling with circulating water was found to be most appropriate. A serum sample, 20μl, absorbed to a small piece of filter paper was applied onto the medium 1cm away from the cathode. Under these conditions, the pH gradient was linear in the range from pH 3.5 to 9.5, and serum proteins were clearly separated.
This method was applied to the separation of γ-GTP isoenzymes. γ-GTP was stained with γ-L-glutamyl-p-diethylaminoanilide. After electrophoresis, the gel was fixed with 50% saturated ammonium sulfate solution followed by removal of the ammonium sulfate, and then submitted to staining procedures. This pretreatment was found to give very clear and permanently preservable electrophoretic patterns. Serum γ-GTP was separeted into 7 isoenzyme bands by this method. The bands which consistently appeared were in pI range of 4.5-5.0, while a band at pI 5.5 was noted in the cases of bile stagnation, and a band at pI 6.5 was observed in cases with malignant tumors.View full abstractDownload PDF (4887K)
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