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Volume 22, Issue 1
Displaying 1-9 of 9 articles from this issue
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Yasuyuki Takagi1993 Volume 22 Issue 1 Pages 2-7
Published: March 31, 1993
Released on J-STAGE: November 27, 2012
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Molecular Analysis of a Dysmyelinating DiseaseAkiko Iwaki, Yasuyuki Fukumaki1993 Volume 22 Issue 1 Pages 8-12
Published: March 31, 1993
Released on J-STAGE: November 27, 2012
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Harutaka Mukoyama1993 Volume 22 Issue 1 Pages 13-20
Published: March 31, 1993
Released on J-STAGE: November 27, 2012
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Nobuyuki Kobayashi1993 Volume 22 Issue 1 Pages 21-28
Published: March 31, 1993
Released on J-STAGE: November 27, 2012
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Yoshifumi Matsuda, Reiko Ishii, Kyousuke Miyazaki, Koichi Takeuchi, Ta ...1993 Volume 22 Issue 1 Pages 29-34
Published: March 31, 1993
Released on J-STAGE: November 27, 2012
JOURNAL FREE ACCESSSmall amounts of arginine amidolytic activity were found to be released from isolated rabbit arteries. The output of specific arginine amidolytic activity (n mol/min/mg wet weight) from the central ear artery was greater than that from the aorta and that from the pulmonary artery, but the output of lysine amidolytic activity was similar for all three of these arteries. With respect to the time course of the enzyme output, arginine and lysine amidolytic activity in the first time period (0-30 min) was higher than that in each of two later time periods. Electrical stimulation at 4 Hz for 3 minutes had no effect on the output of these amidolytic activities from the isolated rabbit arteries. We confirmed using lima bean trypsin inhibitor (LBTI) affinity adsorption and elution that approximately 30% of arginine amidase activity in the isolated aorta preparation was trypsin-like arginine amidase.View full abstractDownload PDF (668K) -
Mayumi Furuta, Hiromi Saito, Toshimasa Nakayama1993 Volume 22 Issue 1 Pages 35-41
Published: March 31, 1993
Released on J-STAGE: November 27, 2012
JOURNAL FREE ACCESSWe studied the difference in glucose levels between capillary (C) and venous (V) whole blood during 75g oral glucose tolerance test (OGTT) in healthy subjects.
The post-loaded glucose levels in capillary blood were significantly higher than those in venous.blood (p<0.01), and the mean values of C-V difference at 30, 60, 90, 120 and 180 min were 24.6, 25.2, 19.3, 17.1 and 9.3, respectively, with the maximum difference at 60 min.
No correlation was found between the magnitude of C-V difference and the levels of glucose in 75 healthy volunteers, although varying C-V differences (-9-52 mg/dl) were observed among them.
Out of 75 subjects 16 had different diagnosis depending on the measurement of either C or V glucose values. Moreover, many subjects, 24 out of 75, were diagnosed to be impaired glucose tolerance (IGT) when evaluated by C blood glucose. These findings indicate that the criteria, recommended by Japan Diabetes Sociaty, for judging C blood glucose levels may be low when compared with those for V glucose.View full abstractDownload PDF (745K) -
Keiko Kawakami, Toshihiko Tsukada, Toshimasa Nakayama1993 Volume 22 Issue 1 Pages 42-48
Published: March 31, 1993
Released on J-STAGE: November 27, 2012
JOURNAL FREE ACCESSNon-linearity in the enzyme immunoassay system for γ-seminoprotein (γ-Sm), Chugai Seiyaku Co., was previously frequently observed for series of diluted patient samples having elevated γ-Sm levels. This was greatly improved by using diluted seurm, inactivated serum, or a two-step modification of the system. The inhibition is presumably the result of the following: since the assay system uses a common one-step sandwich method, γ-Sm and some constituents in serum, possibly including prostate specific antigen (PSA), equally react with enzyme-labeled anti-γ-Sm antibody in the 2nd step of the antigen-antibody reaction. The titer of γ-Sm assayed is then falsely low dye to lack of the labeled reagent. Fairly good linearity was obtained in a recently improved assay system making use of decreased sample volumes and increased labeled antibody. The results of HPLC gel filtration demonstrated that the molecular weight for γ-Sm was mainly 34KD which was in agreement with that described earlier reports, and the fractions for PSA were divided into two portions corresponding to their molecular weights of 34KD and 120KD. The PSA fraction of the 120KD portion inhibited the γ-Sm reaction.View full abstractDownload PDF (705K) -
Yuji Suzuki, Yoshikatsu Sakagishi1993 Volume 22 Issue 1 Pages 49-56
Published: March 31, 1993
Released on J-STAGE: November 27, 2012
JOURNAL FREE ACCESSThe separation and characterization of two kinds of the intermediates formed from bilirubin in the diazo coupling reaction have been undertaken by means of thin layer chromatography on silicagel 70 FM plate-Wako using chloroform/methanol/acetic acid (97: 2: 1, v/v) as a developing solvent. The product extracted from the reaction mixture with chloroform was separated into two yellowish compounds, the intermediate I and II. Comparison of Rf values of the intermediates produced from bilirubin IIIα, IXα and XIIIα in the diazo coupling reaction implied that the intermediate I exhibiting a larger Rf value would be the exovinyl dipyrrole, while the intermediate II would be the endovinyl isomer. In addition, the absorption spectra of these intermediates extracted from silicagel plate with methanol were similar, indicating that bilirubin IXα would be cleaved equally at both sides of the methylene bridge in its molecule. These intermediates reacted with various diazonium salts to form azobilirubins like bilirubin, whereas they underwent oxidation with nitrous acid to yield colorless substance unlike bilirubin. Thus, it has proved that the chemical reactivities of these intermediates are very similar each other.View full abstractDownload PDF (822K) -
Tomojirou Seki1993 Volume 22 Issue 1 Pages 57-59
Published: March 31, 1993
Released on J-STAGE: November 27, 2012
JOURNAL FREE ACCESSMany papers have been published concerning ratio of reactivities of amylase isozymes (P- and S-amylase) to the substrates: oligosaccharide. P-Amy% is the ratio of pancreatic isoamylase to total amylase activity determined by the use of either antibody to isoamylase or amylase inhibitor from wheat germ. We elaborate the method with which P-Amy% is shown in third dimensional way on the conventional scattered diagram, when we make a comparison of two amylase tests that used different substrates. P-Amy% is figured in the open circle with diameter proportional to its value. This third-dimentional scattered diagram shows the ratio of reactivities of isoamylases to the substrates in the tests.View full abstractDownload PDF (230K)
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