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Volume 25 (1979)
- Issue 6 Pages 459-
- Issue 5 Pages 351-
- Issue 4 Pages 269-
- Issue 3 Pages 131-
- Issue 2 Pages 59-
- Issue 1 Pages 1-
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Volume 25, Issue 5
Displaying 1-11 of 11 articles from this issue
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Kenichi KANO, Hisashi YOSHIDA, Junichi YATA, Etsuko ABE, Reiko TANABE, ...1979 Volume 25 Issue 5 Pages 351-360
Published: 1979
Released on J-STAGE: April 28, 2009
JOURNAL FREE ACCESSAn assay method for separately measuring the metabolites of vitamin D2 and D3 is investigated. Seven-week-old Wistar male rats were orally administered 200-20, 000IU of either vitamin D2 or D3 on alternate days for 12 days. The blood plasma was extracted with either methanol-chloroform for 25-OH-D and 24, 25-(OH)2-D, or dichloro-methane for 1α, 25-(OH)2-D. Each extract was applied separately to Sephadex LH-20 columns and then to high pressure liquid chromatog-raphy (HPLC). On HPLC each D2 metabolite appeared to be eluted in the region just prior to the respective D3 metabolite. 25-OH-D3, 24, 25-(OH)2-D3, and metabolites presumed to be 25-OH-D2 and 24, 25-(OH)2-D2 were measured separately by a competitive protein binding assay using rachitic rat plasma. 1α, 25-(OH)2-D3 and a metabolite suspected to be 1α, 25-(OH)2-D2 were determined by Eisman's radioreceptor assay. When the rats were given graded amounts of D3 for 12 days, plasma levels of 25-OH-D3 and 24, 25-(OH)2-D3 increased in proportion to the dose levels of D3, while those of 1α, 25-(OH)2-D3 remained unchanged. The plasma levels of 24, 25-(OH)2-D3 correlated closely with those of 25-OH-D3 (γ=0.978). Hypercalcemia induced by high doses of D3 appeared to be due to the increase of 25-OH-D3 rather than to 1α, 25-(OH)2-D3.View full abstractDownload PDF (914K) -
Sei TACHIBANA, Masanori OKA, Hitomi TAMURA, Atsuko KAMEI, Harumi MUKAI ...1979 Volume 25 Issue 5 Pages 361-366
Published: 1979
Released on J-STAGE: April 28, 2009
JOURNAL FREE ACCESSThe microbial activities of vitamin B2-aldehyde and vitamin B2-acid, produced by Schizophyllum commune, a Basidiomycete, were studied. Lactobacillus casei ATCC No. 7469 was used as a test microorganism. B2-aldehyde exhibited a good response curve in the growth of L. casei. B2-acid had neither a stimulatory nor an inhibitory effect on the growth. When B2-aldehyde was incubated with the homogenate of L. casei, it was converted to riboflavin. The flavin formed from B2-aldehyde by the homogenate not only exhibited an equivalent response curve to authentic riboflavin in the growth of L. casei, but also showed the same Rf value as authentic riboflavin in any paper chromatogram, as far as tested. Hence, the microbial activity of B2-aldehyde for L. casei seems to be ascribable to riboflavin which is a reduction product of B2-aldehyde.View full abstractDownload PDF (539K) -
Michio HOSHINO, Tadashi ASAKURA, Makoto MATSUDA1979 Volume 25 Issue 5 Pages 367-374
Published: 1979
Released on J-STAGE: April 28, 2009
JOURNAL FREE ACCESSThe in vivo effect of semicarbazide (SC) and aminoxyacetic acid (AOAA) upon γ-aminobutyric acid (GABA) levels in the synapto-somal fraction, and GABA release from the same fraction were studied in the mouse. The convulsive dose of SC reduced the GABA content in synaptosomes, and when the convulsions were protected by pretreatment with AOAA, the reduced GABA content in synaptosomes rose to or above the normal level. Moreover, the SC treatment decreased the GABA releases from synaptosomes both in a Ca2+-free Ringer's solution and in a high K+ Ringer's solution. When the convulsions were protected by pretreatment with AOAA, the decreased GABA releases in both the conditions rose to or above the normal levels. Therefore, it is suggested that the decrease in GABA release from the nerve endings, because of the decrease of GABA content in the same compartment, is possibly an important factor in the onset of some kinds of convulsions.View full abstractDownload PDF (830K) -
Tomoko ABE, Eiichi OKAMOTO, Yoshinori ITOKAWA1979 Volume 25 Issue 5 Pages 375-383
Published: 1979
Released on J-STAGE: April 28, 2009
JOURNAL FREE ACCESSRats were separated into four groups and four different liquid diets were given to each group. Group l: thiamine-sufficient diet with no ethanol, group 2: thiamine-sufficient diet with ethanol, group 3: thiamine-deficient diet with no ethanol, group 4: thiamine-deficient diet with ethanol. After four weeks, all rats were fasted for 24 hr and then ethanol was given orally to every rat. After one hour, every rat was sacrificed and biochemical and histological analyses were carried out. Transketolase activity in brain and liver decreased in groups 2, 3 and 4. There was significant decrease in transketolase activity in ethanol-fed groups (groups 2 and 4) as compared to control groups (groups 1 and 3). Ethanol concentrations in blood, liver and heart of rats in groups 2 and 4 were higher than in groups 1 and 3. When comparison was made between the thiamine-deficient groups and the corresponding thiamine-sufficient groups, ethanol concentrations in liver and heart were higher in the thiamine-deficient groups. Alcohol dehydrogenase activity in liver decreased significantly in groups 2 and 4. By histological analyses, fatty degeneration was observed in the livers of groups 2 and 4. The degeneration was more prominent in group 4 than group 2. These findings suggest that chronic ethanol administration may impair the ability to metabolize ethanol and the impairment may increase when rats are in the condition of thiamine deficiency.View full abstractDownload PDF (4893K) -
Katsuji TAKADA, Toshio OKANO, Yoko TAMURA, Sachiko MATSUI, Tadashi KOB ...1979 Volume 25 Issue 5 Pages 385-398
Published: 1979
Released on J-STAGE: April 28, 2009
JOURNAL FREE ACCESSIn order to develop the investigations into photobiogenesis of vitamin D3, a rapid and precise method for the determination of the vitamin in rat skin was established by using high-performance liquid chromatography (HPLC). The proposed method included saponification of small pieces of rat skin, extraction of the unsaponifiable matter and application to HPLC using “Zorbax SIL” (straight-phase) as an adsorbent and 0.5% isopropanol in n-hexane as a mobile phase. The applicable lower limit of the method was 2ng of vitamin D3/cm2 of subcutaneous tissue-removed skin and it was possible to assay a concentration higher than 2ng/cm2. The proposed method was applied to determine the content of vitamin D3 in rat skin obtained from in vivo and in vitro irradiation experiments. In the in vitro experiment, the yield of vitamin D3 increased in proportion to the irradiation time. On the other hand, the yield in the in vivo experiment showed a proportional increase similar to the in vitro experiment until 60min irradiation, while a nearly constant value was obtained by irradiation for longer than 60min. When the rat skin obtained from the in vitro experiment was irradiated with monochromatic UV rays in the range 260-350nm, the most effective wavelength for the formation of vitamin D3 was confirmed to be 303nm, which differs from the result obtained from the experiment in a test tube (295nm). Moreover, the yield of vitamin D3 by irradiation with UV rays below 288nm was extremely low, which again differed from the results of a test tube experiment. These differences were thought to be due to the filter effect of the malpighian layer in the epidermis of rat skin.View full abstractDownload PDF (1207K) -
Fumio SHIMURA, Sachiko MORIUCHI, Norimasa HOSOYA1979 Volume 25 Issue 5 Pages 399-409
Published: 1979
Released on J-STAGE: April 28, 2009
JOURNAL FREE ACCESSThe interaction of 1α, 24-dihydroxyvitamin D3 with the 1α, 25-dihydroxyvitamin D3 receptor system was studied in chick intestinal mucosa.
The competitive receptor binding assay indicated that 1α, 24-dihydroxy-vitamin D3 bound to a cytosol 1α, 25-dihydroxyvitamin D3 receptor with a relatively high affinity compared with other vitamin D3 analogs. The R-isomer of 1α, 24-dihydroxyvitamin D3 revealed higher affinity for the receptor than the S-isomer.
In the reconstituted cytosol-chromatin system, both 1α, 24(R)-dihydroxy-[3H]-vitamin D3 and 1α, 24(S)-dihydroxy-[3H]-vitamin D3 specifically associated with chromatin via a temperature-dependent process. The association of 1α, 24-dihydroxy-[3H]-vitamin D3 with chromatin was reduced in the presence of competing unlabeled 1α, 25-dihydroxyvitamin D3. Furthermore, the chromatin-associated 1α, 24-dihydroxy-[3H]-vitamin D3 was dissociated by a high concentration of KCl, likewise 1α, 25-dihydroxy-[3H]-vitamin D3.
From these results, it is strongly indicated that 1α, 24-dihydroxyvitamin D3 is recognized by cytosol 1α, 25-dihydroxyvitamin D3 receptor as an analog of 1α, 25-dihydroxyvitamin D3 and associates with chromatin by the same mechanism as 1α, 25-dihydroxyvitamin D3.View full abstractDownload PDF (1027K) -
Fumi YOKOTA, Nobuo MATSUNO, Ryokuero SUZUE1979 Volume 25 Issue 5 Pages 411-417
Published: 1979
Released on J-STAGE: April 28, 2009
JOURNAL FREE ACCESSAn experiment was performed to investigate the progressive changes of the anemia caused by excess methionine in rats, during the developmental and convalescent periods. Hemoglobin con-centration, hematocrit value and red blood cell count were elevated in the initial stage of excess methionine feeding, they then gradually decreased. During the convalescent period, after ceasing administration of the excess methionine diet, symptoms of anemia gradually disappeared. The nitrogen efficiency ratio was markedly decreased by excess methionine feeding, however, it rapidly recovered after ceasing administration of the excess methionine diet. Iron deposited in the spleen also disappeared quickly during the convalescent period. Of the symptoms of anemia caused by excess methionine, the activity of δ-aminolevulinic acid synthetase (ALAS) in the bone marrow showed the most acute changes. As mentioned previously (1), although lowered globin biosynthesis due to amino acid imbalance could be considered as one of the important causes of the anemia and also would be one of the causes of the compensative elevation of ALAS activity, the possibility still remain that there are other unknown effects of excess methionine on ALAS activity in the bone marrow in this case.View full abstractDownload PDF (524K) -
Yasuo KASUBUCHI, Masahiro MINO, Hiroshi YOSHIOKA, Tomoichi KUSUNOKI1979 Volume 25 Issue 5 Pages 419-426
Published: 1979
Released on J-STAGE: April 28, 2009
JOURNAL FREE ACCESSThe renewal of adipose cells in adult mice has been autoradiographically studied. The number of adipose cells was dimin-ished by eighty percent during malnutrition and the same number of adipose cells proliferated during the refeeding stage. The results of our study showed that adipose tissue, which had previously been believed to be stable in cell number, has the capacity for cell proliferation according to changes in nutritional status.View full abstractDownload PDF (2500K) -
Yoshiaki FUJITA, Takashi YAMAMOTO, Toru RIKIMARU, Goro INOUE1979 Volume 25 Issue 5 Pages 427-439
Published: 1979
Released on J-STAGE: April 28, 2009
JOURNAL FREE ACCESSStudies were made on alterations in plasma amino acids in young men fed a diet containing graded levels of wheat gluten. After one week on a standard diet containing 200mgN/kg of mixed protein (animal protein content 45%), 38 young men were given a wheat gluten diet containing 170, 100, 60, 30, 15 or zero mgN/kg for 2 weeks. Blood samples measuring plasma free amino acids were taken before breakfast at the end of the periods on a standard diet and an experimental diet. In subjects on diets containing 170 to 30mgN/kg the plasma concentrations of threonine, valine, methionine, leucine, tyrosine, phenylalanine, serine, histidine and arginine fell significantly with decrease in protein intake, but the concentration of alanine increased significantly. On the other hand, in subjects on diets containing 15 or zero mgN/kg, the plasma con-centrations of the essential amino acids did not decrease, but increased to slightly more than in subjects on a diet containing 30mgN/kg, and the alanine and glycine concentrations increased steadily. Values for plasma lysine varied from 146±22 to 194±31 μmoles/liter with gluten intakes of 170 to zero mgN/kg, but were comparable with that of 186±33 μmoles/liter in subjects on a standard diet, showing that the plasma lysine concentration did not clearly reflect the dietary concentration of lysine in young men on a wheat gluten diet.View full abstractDownload PDF (1166K) -
Toshizo KIMURA, Fumihiko HORIO, Akira YOSHIDA1979 Volume 25 Issue 5 Pages 441-453
Published: 1979
Released on J-STAGE: April 28, 2009
JOURNAL FREE ACCESSIn order to investigate the relationship between dietary amino acids and protein, as well as the activities of intestinal sucrase and leucine aminopeptidase in rats, the effects of an amino acid imbalance on these enzyme activities were studied. The amino acid imbalance was created by adding 8% of an indispensable amino acid mixture lacking threonine to a 6% casein diet supplemented with 0.3% methionine. The food intake and growth of rats fed the imbalanced diet ad libitum were depressed, and the segmental weights of the small intestine and its sucrase activity were clearly lower than those of rats fed the basal diet. The effect of the imbalanced diet under pair-feeding condition on the sucrase activity was similar to that under an ad libitum feeding condition. The food intake and segmental sucrase activity, that is, sucrase activity per length of the small intestine, of rats injected with cortisol (1mg/day) and fed the imbalanced diet were not depressed, although administration of insulin (1.5U/day) had no effect on the food intake or segmental sucrase activity. Force-feeding stimulated growth of rats receiving the imbalanced diet, as well as increasing their segmental sucrase activities. The effects of these different conditions on the leucine aminopeptidase activity of rats receiving the imbalanced diet were obscure. These results suggest that changes in segmental sucrase activity might be mediated by stimulating factors in food intake affected by the composition of ingested amino acids and protein together with sucrose in the gastrointestinal lumen.View full abstractDownload PDF (1311K) -
Sachiko MORIUCHI, Fukiko TSURUKI, Yoko OTAWARA, Norimasa HOSOYA, Sachi ...1979 Volume 25 Issue 5 Pages 455-458
Published: 1979
Released on J-STAGE: April 28, 2009
JOURNAL FREE ACCESSDownload PDF (316K)
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