Japanese Journal of Clinical Chemistry
Online ISSN : 2187-4077
Print ISSN : 0370-5633
ISSN-L : 0370-5633
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Volume 11, Issue 3
Displaying 1-14 of 14 articles from this issue
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  • Lipoprotein Analysis
    AKIRA YAMAMOTO
    1982 Volume 11 Issue 3 Pages 161-165
    Published: October 25, 1982
    Released on J-STAGE: November 27, 2012
    DOIhttps://doi.org/10.14921/jscc1971b.11.3_161
    JOURNAL FREE ACCESS
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  • Application of High Performance Liquid Chromatography on the Quantitation of Serum Lipoproteins
    ICHIRO HARA
    1982 Volume 11 Issue 3 Pages 166-172
    Published: October 25, 1982
    Released on J-STAGE: November 27, 2012
    DOIhttps://doi.org/10.14921/jscc1971b.11.3_166
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  • Cross-Linking Studies on the Structure of High Density Lipoprotein
    YOUICHI YACHIDA, OSAMU MINARI
    1982 Volume 11 Issue 3 Pages 173-181
    Published: October 25, 1982
    Released on J-STAGE: November 27, 2012
    DOIhttps://doi.org/10.14921/jscc1971b.11.3_173
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  • Radioimmunoassay of Apolipoprotein A-I and A-II of Human High Density Lipoprotein
    SHOICHI AKAZAWA, TOSHIAKI NAKANISHI, SEIBEI MIYAKE, SHIGENOBU NAGATAKI
    1982 Volume 11 Issue 3 Pages 182-187
    Published: October 25, 1982
    Released on J-STAGE: November 27, 2012
    DOIhttps://doi.org/10.14921/jscc1971b.11.3_182
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  • Determination of HbAlc by High Performance Liquid Chromatography Based on Hydrophobic Interaction
    TOSHIHIRO AKAI, KEIICHI NAKA, KIYOSHI OKUDA, SATORU FUJII, KAZUTOSHI Y ...
    1982 Volume 11 Issue 3 Pages 188-193
    Published: October 25, 1982
    Released on J-STAGE: November 27, 2012
    DOIhttps://doi.org/10.14921/jscc1971b.11.3_188
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    A new HPLC (High Performance Liquid Chromatography) method for the determination of HbAlc (Hemoglobin Alc) is proposed. This method uses the hydrophobic stationary phase, which can separate minor components of hemoglobin more clearly than the previous method.
    As this stationary phase is hard enough to bear high pressure, precise data has been achieved for many loadings.
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  • Anomeric Preference of Maltose Hydrolysis by the Brush Border-Bound Maltase from the Rat Small Intestine
    KAZUO MAEDA, ICHITOMO MIWA, JUN OKUDA
    1982 Volume 11 Issue 3 Pages 194-199
    Published: October 25, 1982
    Released on J-STAGE: November 27, 2012
    DOIhttps://doi.org/10.14921/jscc1971b.11.3_194
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    The Km value (0.ssmM) of the brush border-bound maltase from the rat small intestine for a-maltose was lower than that (2.3mM) for β-maltose, whereas the Vmax values for both anomers were the same. Thus, at finite concentrations, α-maltose was better hydrolyzed than β-maltose by the enzyme. This α-anomeric preference seemed to be purposive in starch digestion because pancreatic α-amylase is known to produce maltose in the a form from starch. A modification, utilizing fluorometry of NADH, of a spectrophotometric method for the assay of glucose anomers with β-D-glucose dehydrogenase and mutarotase was developed and applied to the anomer analysis of the glucose released by hydrolysis of maltose by the brush border-bound maltase. The glucose of the non-reducing end was released exclusively in the a form: i.e., almost entirely pure a-Dglucose was produced from a-maltose. The data obtained in this study were discussed in relation to the transport mechanism of the glucose liberated from maltose.
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  • Clinical Application of Purine Metabolic Enzyme Activities in Sera
    KENJI KATO, TETSUO ADACHI, YOSHIMASA ITO, KAZUYUKI HIRANO, MAMORU SUGI ...
    1982 Volume 11 Issue 3 Pages 200-206
    Published: October 25, 1982
    Released on J-STAGE: November 27, 2012
    DOIhttps://doi.org/10.14921/jscc1971b.11.3_200
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    Adenosine deaminase, purine nucleoside phosphorylase and guanase activities in sera of patients with various diseases were determined by the new colorimetric methods.
    It was observed that the serum guanase activity increased specifically in liver disorders and correlated with serum transaminase activity. Although the serum adenosine deaminase activity also increased in liver diseases, the clinical value of adenosine deaminase may be different from that of guanase.
    It was found that the serum purine nucleoside phosphorylase activity, which increased in patients with malignant lymphoma and systemic lupus erythematosus, correlated with the amount of sensitized lymphocyte.
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  • Effects of Transferrin and Ceruloplasmin on Liver Microsomal Lipid Peroxidation
    ISAO ISHIGURO, YOSHIJI OHTA, NAOMICHI OGITSU, YOSHINORI ITO, JIRO HARA ...
    1982 Volume 11 Issue 3 Pages 207-213
    Published: October 25, 1982
    Released on J-STAGE: November 27, 2012
    DOIhttps://doi.org/10.14921/jscc1971b.11.3_207
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    Transferrin (Tf) and ceruloplasmin (Cp) in human serum are found to strongly inhibit lipid peroxidation by rat liver microsomes, and a study was made of this inhibition. Apo-Tf strongly inhibited NADPH dependent and ascorbic acid dependent lipid peroxidations of microsome. However, the inhibition of apo-Tf almost disappeared by adding iron ion to the system of the reaction. Inhibition of holo-Tf formed by adding Fe3+ to apo-Tf was mar kedly decreased. As a result of this, it was inferred that inhibition of apo-Tf is due to bon ding with iron ion necessary for lipid peroxidation in microsome. Cp showed a stronger in hibition than apo-Tf. It was confirmed that inhibition of Cp is due to oxidation of Fe2+, which is necessary for lipid peroxidation of microsome, into Fe3+ by ferroxidase action of Cp.
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  • A New Method of Serum Mucoprotein (Acid Soluble Glycoproteins: ASP) Assay Using Coomassie Brilliant Blue G-250
    KATSUYUKI NAKAJIMA, TSUKASA KODAIRA, YUTAKA ICHIOKA, HIRONORI NITTA, H ...
    1982 Volume 11 Issue 3 Pages 214-221
    Published: October 25, 1982
    Released on J-STAGE: November 27, 2012
    DOIhttps://doi.org/10.14921/jscc1971b.11.3_214
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    A new and simple method for protein assay in strongly acidic solution was developed and applied to the assay of perchloric acid soluble glycoproteins (ASP) in serum. Serum ASP levels were determined directly with the supernatants deproteinized by 0.6M perchloric acid using Coomassie Brilliant Blue G-250. This method required neither pH neutralization nor further precipitation of ASP by phosphotungstic acid.
    The comparative studies of ASP and seromucoid fraction have shown that the composi tion of both protein fractions was almost identical. Also the serum levels of ASP was highly correlated with seromucoid levels by Winzler method. The results suggest that ASP determi nation by C.B.B.-G-250 method is thought to be identical with serum mucoprotein assay.
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  • Estimation of Serum Free-Thyroxine Concentration by Solidphase Antibody Radioimmunoassay (AMERLEX® FREE T4)
    Comparison with Computational Analysis and Its Clinical Application
    KEIKO NISHI, KIYOSHI ICHIHARA, KEI DOI, KIYOMI NAKATANI, MARIKO IKEUCH ...
    1982 Volume 11 Issue 3 Pages 222-230
    Published: October 25, 1982
    Released on J-STAGE: November 27, 2012
    DOIhttps://doi.org/10.14921/jscc1971b.11.3_222
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    A new radioimmunoassay method (Amerlex® Free T4) for measurement of the serum concentration of free thyroxine (FT4) was evaluated with the following results.
    1. The estimated values were almost constant during incubation for 30 to 240 min at37°C.
    2. The coefficients of variation, which were 2.5-3.5% (within assay) and 5.2-16.5% (between assays), were acceptable for clinical tests.
    3. The FT4 values of sera with added T4 determined by this method were identical to those estimated by computational analysis.
    4. The FT4 concentration determined by this method in normal sera was 1.42±0.24ng/dl (normal range: 0.90-1.90ng/dl). The serum FT4 concentration was increased in hyperthyroidism, decreased in hypothyroidism, at the lower limit of normal in pregnancy (18-26 weeks) and liver cirrhosis, and within normal limits in familial TBG excess and TBG deftciency.
    5. The FT4 values determined by this method correlated well with those determined by computational analysis, and equilibrium dialysis and with the FT4 index.
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  • Determination of Purine Metabolites in Serum and Urine by High Performance Liquid Chromatography
    TSUKASA KOJIMA, ITOKO IIMORI, TOSHIHIRO NISHINA, MOTOSHI KITAMURA, KUS ...
    1982 Volume 11 Issue 3 Pages 231-236
    Published: October 25, 1982
    Released on J-STAGE: November 27, 2012
    DOIhttps://doi.org/10.14921/jscc1971b.11.3_231
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    A reverse phase high performance liquid chromatography (HPLC) method was developed for the determination of Hypoxanthine, Xanthine, Uric acid, Allopurinol (4-hydroxypyrazolo-(3, 4-d) pyrimidine) and Oxypurinol (4, 6-dihydroxypyrazolo-(3, 4-d) pyrimidine) in human serum and urine.
    This technique is as follows: Speciments were deproteinized with Amicon centriflo membrane cone type CF25 (Amicon Corp.) and were injected into the HPLC column directly. 0.04mol/l phosphate buffer, pH 2.2, contained 2% methanol (V/V) was used as the mobilphase and the eluent were monitored at 254nm.
    Proposed method, which has good sensitivity (the lower limites of determination 1.0 μmol/l for the compounds), precision (CV, 2-3% for 100 μmol/l compounds) and accuracy (almost 100% recovery), were observed.
    This method should be useful in the clinical studies for abnormal purine metabolism.
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  • The Rapid and Simple Determination of Urinary 3-Methoxy-4-Hydroxymandelic Acid Eliminated the Interference of Exogenous Vanillin
    JUNICHI IWAMURA, MAGOHEI YAMADA, KAZUTAKA ARISUE, KAZUMA KOHDA, CHOZO ...
    1982 Volume 11 Issue 3 Pages 237-243
    Published: October 25, 1982
    Released on J-STAGE: November 27, 2012
    DOIhttps://doi.org/10.14921/jscc1971b.11.3_237
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    Methods for a determination of 3-methoxy-4-hydroxy-mandelic acid (VMA) based on the Pisanos' method are complicated and time consuming, so the convenal method is modified to simplify and increase speed of an analysis. The procedure can eliminate interfering substances (for example, vanillin) from urine by the pre-extraction using ethyl acetate, and the treatment for oxidation with periodic acid to convert VMA to vanillin is performed at the room tempareture. Vanillin which formed is extracted with toluene, followed by the extraction with 1M potassium carbonate solution, and then absorbance of the potassium carbonate layer is determined spectrophotometrically.
    The coefficient of variation between the Pisano's method and the proposed method was 0.95, and mean recovery of standerd added to urine was 99.8 per cent (n=21).
    The determination of VMA, the end-product of catecholamine metabolism, is important for diagnosis of patients with pheochromocytoma, ganglioneuroma, neuroblastoma, metastatic carcinoid, and familial dysautonomia, etc, so this modified simple method is useful for the clinical test.
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  • Simple and Rapid Method for Determination of Arginase Activity in a Dried Blood Spot on Filter Paper and Hemolysate
    YOKO NISHIKAWA, FUKUKO WATANABE
    1982 Volume 11 Issue 3 Pages 244-248
    Published: October 25, 1982
    Released on J-STAGE: November 27, 2012
    DOIhttps://doi.org/10.14921/jscc1971b.11.3_244
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    A semi-automated method for arginase activity in a dried blood spot and hemolysate is described. Urea produced by arginase action was measured with the enzymes of urease and glutamate dehydrogenase, 2-oxoglutarate and NADH. The decrease in absorbance at 340nm at 30°C was measured by a centrifugal analyzer, the Centrifichem 400. The conditions of activation with Mn2+, incubation and urea determination are discussed. In dried blood spots, elution of erythrocyte and activation of arginase were performed by incubating discs at 37°C for 30min. We used 25mmol/L MnCI2 to activate and 150mmol/L arginine as substrate to obtain the maximum velocity of arginase activity. As HCIO4 was used for the stopper of the enzyme reaction, pH adjustment for the following enzymatic urea determination could be ommited. Linearity and reproducibility were acceptable. The correlation between arginase activities from dried blood disc and hemolysate in the same subjects was r=0.953. The reference values were 41.7±7.75U/g·Hb in dried blood disc and 39.3±9.44 U/g·Hb (mean±SD, n=20) in hemolysate. The activity from dried blood spot is stable at room temperature for one week, which allows to be mailed.
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  • Determination of Dityrosine in Insoluble Protein by Cation-Exchange High-Performance Liquid Chromatography with Fluorescence Detection
    SEIJI ETO, KIYOSHI ZAITSU, YOSUKE OHKURA
    1982 Volume 11 Issue 3 Pages 249-252
    Published: October 25, 1982
    Released on J-STAGE: November 27, 2012
    DOIhttps://doi.org/10.14921/jscc1971b.11.3_249
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    A cation-exchange high-performance liquid chromatographic method for the sensitive determination of dityrosine in hydrochloric acid-hydrolysate of insoluble protein is described. The method is based on the clean-up of the acid hydrolysate by Dowex 1×8 column chromatography and the separation of dityrosine in the eluate from the column by high-performance liquid chromatography with fluorescence detection on Hitachi Gell 3011-S. The limit of detection for dityrosine is 0.6 pmol per 10μl (the injecton volume) of the sample solution for the chromatography. This method permited the determination of dityrosine in collagen from cow skins and tendons, and should be useful for the determination of dityrosine in various tissues in biological samples.
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