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Volume 42, Issue 12
Displaying 1-5 of 5 articles from this issue
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Renju MAEDA1967 Volume 42 Issue 12 Pages 1302-1311,1297
Published: March 20, 1967
Released on J-STAGE: September 24, 2012
JOURNAL FREE ACCESSA simple method for measurement of thyroxine-binding proteins (TBP) was studied, using cellulose acetate membrane as supporting medium for zone electrophoresis.
Electrophoresis was performed at room temperature in Oxoid cellulose acetate membrane. Nine strips, each 2 by 7 cm. in size, were suspended horizontally in a closed system between plastic plates. The ends were connected by filter papers with two vessels, each containing 240 ml. of buffer. Buffers employed were barbital and tris-maleate, both at pH 8.6. In conventional method, thyroxine (T4) -serum mixture was applied in a band, 2 cm. from the cathodalend of the strip and in a reverse-flow method, 1.5cm. from the anodal end. Electric current was kept constant, i.e. 0.4 mA/width of lcm of the strip. All other conditions were the same as the ordinary electrophoresis in the both methods. Time for electrophoresis was 40-50 min. Low background beta counter with anticoincidence circuit was used in the measurement of trace amount of radiothyroxine. The proteins on the strips were stained with Ponceau 3R. A satisfactory separation could be achieved in radioautograph of TBP without distortion of bands. In barbital, when this method is used to measure the affinity of TBP, both conventional and reverse-flow methods can be used. To measure the maximum capacity of thyroxine-binding globulin (TBG), reverse-flow method was necessary.
With the conventional method employing tris-maleate buffer, the capacity of TBG and T4-binding prealbumin (TBPA) was not obtained due to trailing of protein-bound T4. Radioactivity measurement of TBP was done before and after staining of proteins in the same normal serum to which was added T4 1.0 and 3.2 μg/ml. T4 distribution of TBP was compared and found not to be altered between nonstained and stained rogups. The result suggested a safe staining procedure not affecting T4 distribution of TBP. T4 distribution among proteins at several levels to which T4 was added was also studied in barbital and tris-maleate buffers, and the mean values for the affinity and capacity of TBP in 18 normal adults by the present method were as follows :
The affinity in barbital buffer at added T4 0.002 μg/ml. Conventional : TBG 80%, Albumin 16%. Reverse-flow : TBG 79%, Albumin 18%.
In tris-maleate buffer, TBG 67%, Albumin 14%, TBPA 20%. The capacity of TBG in barbital buffer was 0.22±0.03 (Mean±S.D.) μg/ml, with a range of 0.18-0.26 μglml. The capacity of TBG in 10 cases with untreated hyperthyroidism was nearly within normal limits, while in untreated hypothyroidism the capacity was high in 4 out of 6 cases.
The above results proved the present method is a simple, rapid and reliable technique for clinical use in place of commonly used paper electrophoresis.View full abstractDownload PDF (1638K) -
Masahisa NANAHOSHI1967 Volume 42 Issue 12 Pages 1312-1319,1299
Published: March 20, 1967
Released on J-STAGE: September 24, 2012
JOURNAL FREE ACCESSThis report deals with the effect of glycyrrhizin on the following cortisone actions : anti-inflammatory action (anti-granulomatous and anti-exudative), liver glycogen deposition, liver tryptophan pyrrolase induction, thymic involution, and suppression of antibody formation.
Adult female adrenalectomized rats were used throughout the experiment but for anti-exudative action. In each experiment, animals were divided into four groups : 1) control group, 2) cortisone group, 3) glycyrrhizin group, 4) cortisone + glycyrrhizin group. After the treatment for 6 to 8 successive days, the effect of glycyrrhizin was examined on the above-mentioned cortisone actions.
The anti-granulomatous action of cortisone was : demonstrated to be inhibited by glycyrrhizin using cotton pellet method. A parallel quantitative relationship was shown to exist between the dosage of glycyrrhizin and its inhibitory effect.
The suppressive action of prednisolone on in vitro proliferation of L cell was also blocked by glycyrrhizin.
The anti-exudative action of cortisone was hardly affected by concomittant administration of glycyrrhizin even in large doses following granuloma pouch method.
Either liver glycogen deposition, liver tryptophan pyrrolase induction or thymic involution was significantly inhibited by glycyrrhizin.
In contrast to the actions described above, glycyrrhizin was found to enhance the suppressive effect of cortisone on antibody formation against bacterial amylase as an antigen.View full abstractDownload PDF (919K) -
Shibanosuke KATSUKI, Sakurai ANDO, Shigeyoshi YUJI, Shigenobu KONDO, S ...1967 Volume 42 Issue 12 Pages 1320-1325,1300
Published: March 20, 1967
Released on J-STAGE: September 24, 2012
JOURNAL FREE ACCESSWood et al. (1965) reports that response of cortisol secretion to single intramuscular injection of synthetic polypeptide can be used as a test of adrenocortical function. This report concerns our experience with this test carried out in 107 cases.
The first blood sample was drawn at 9 a.m., immediately followed by intramuscular injection of 250 μg of synthetic 24 amino acid polypeptide (β1-24-corticotropin, CIBA 30'920-Ba). Thirty minutes thereafter, the second blood sample was taken. After centrifugation of blood samples, plasma 11-OHCS was determined by the fluorimetric method of De Moor et al..
In 21 control subjects, plasma 11-OFICS level was 9.8±3.1 μg/dl (mean±S.D.) before synthetic polypeptide injection, which rose to 20.4±4.1 /μg/dl 30 minutes after the injection. The response was subnormal or markedly suppressed in patients receiving glucocorticoid therapy, Addison's disease and Sheehan's syndrome, but it was definitely augmented in 2 out of 4 cases with Cushing's syndrome.
Our experience indicates that the rapid test proposed by Wood et al. is useful as a screening test for adrenocortical function. No side effects were seen during the test procedure.View full abstractDownload PDF (605K) -
Yoshio IKEDA, Shoichi KOYAMA, Tomio TANESE, Masakazu ABE1967 Volume 42 Issue 12 Pages 1326-1333,1301
Published: March 20, 1967
Released on J-STAGE: September 24, 2012
JOURNAL FREE ACCESSResults of in vitro and in vivo experiments on the action of adrenal cortical steroid hormone on the metabolism of adipose tissue have indicated that the hormone inhibits glucose utilization in adipose tissue.
The present paper summarizes the results of our experiments, both in vitro and in vivo, on the effect of β-methazone, a synthetic adrenal cortical steroid, on glucose uptake and insulin effect in epididymal adipose tissue of the rat.
1) β-methazone (0.001 γ-10 γ/ml) did not effect any significant change when the medium in which the adipose tissue was immersed did not contain albumin, however, the stimulating effect of insulin (10 μu-1.000 μu/ml) on glucose uptake was definitely inhibited.
2) When 2% albumin was added to the medium, β-methazone increased glucose uptake of adipose tissue, and simultaneously, increased the release of free fatty acid into the medium. These effects were not influenced by the glucose concentration of the medium or by the incubation time.
3) The insulin effect in adipose tissue was also not inhibited by the addition of β- methazone when albumin was present in the medium. However, regarding the release of free fatty acid, β-methazone acted antagonistically to insulin.
4) Basal glucose uptake and insulin sensitivity of the tissues were studied in the epididymal adipose tissue of rats which had been given β-methazone 1 mg., daily, for 3 consecutive days prior to extirpation. No significant difference in treated group and the control group, however, a decrease in insulin sensitivity was observed in the β-methazone group.
Based on the results of the aforementioned experiments, a few considerations were made on the influence of corticosteroid hormones on adipose tissue metabolism, and suggestions were made that the imbalance between lipolytic hormones such as the hypophyseal, adrenal cortical hormones and insulin may be one of the causative factors in the pathogenesis of diabetes mellitus.View full abstractDownload PDF (1095K) -
1967 Volume 42 Issue 12 Pages 1334-1389
Published: March 20, 1967
Released on J-STAGE: September 24, 2012
JOURNAL FREE ACCESSDownload PDF (9056K)
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