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Volume 25, Issue 1
Displaying 1-7 of 7 articles from this issue
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Mayumi SATO, Masahide OMORI, Yasutoshi MUTO1979 Volume 25 Issue 1 Pages 1-7
Published: 1979
Released on J-STAGE: April 28, 2009
JOURNAL FREE ACCESSBy sucrose density gradient sedimentation analysis, a cytosol component of small molecular size which bound 3H-retinoic acid was detected in the chick embryo brain, exhibiting a peak on day 14 (7 days before hatching). In general, cellular retinol-binding protein (CRBP) and cellular retinoic acid-binding protein (CRABP) have been distin-guished by showing binding specificity for retinol or retinoic acid, respectively. However, the component found in embryo brain cytosol exhibited binding affinity for both retinol and retinoic acid, being similar in less ligand-specificity to CRBP (F) which was originally recognized in fish eye cytosol. Moreover, the component also showed a lack of binding affinity for prealbumin (PA), excluding the possibility that chicken plasma RBP was contaminated in the cytosol. These findings strongly suggest that a distinct molecular species of cellular binding protein for vitamin A exists in the brain cytosol of a developing chick embryo.View full abstractDownload PDF (758K) -
Che-Hui KUO, Norifumi YONEHARA, Hiroshi YOSHIDA1979 Volume 25 Issue 1 Pages 9-13
Published: 1979
Released on J-STAGE: April 28, 2009
JOURNAL FREE ACCESSIn scorbutic guinea pigs fed an ascorbic acid-deficient diet for 18 days, the ascorbic acid contents of the liver and plasma were less than 4% those of the control animals, while the content in the brain was about one-third that of the controls. In normal animals, the concentration of ascorbic acid was highest (7.55±1.46μg of ascorbic acid/mg protein) in the S3 fraction and was also fairly high (5.37±0.91) in the P2p fraction (cytoplasm of nerve terminals). During ascorbic acid deficiency, the contents in the P2p and microsome fractions decreased slightly faster than those in other fractions. Even after 18 days' deficiency, no significant change was found in the acetylcholine content of the brain.View full abstractDownload PDF (489K) -
Junko YAMASHITA, Yukio HIRATA1979 Volume 25 Issue 1 Pages 15-22
Published: 1979
Released on J-STAGE: April 28, 2009
JOURNAL FREE ACCESSThe present experiment was performed to examine the relationship between the content of γ-aminobutyric acid of the superior colliculus and running fits induced by injection of semicarbazide (SC), an antivitamin B6, into the superior colliculus of the mouse.
(1) The distribution of 4-aminobutyrate: 2-oxoglutarate aminotransferase [EC 2.6.1.19] of the superior colliculus was studied histochemically. A high activity was observed in the superficial and medial gray layers of the superior colliculus. Pretreatment with aminooxyacetic acid at a dose which inhibits running fits induced by intracollicular injection of SC depressed the activity. (2) The contents of γ-aminobutyric acid in superior colliculi of mice which received an intracollicular injection of SC were 60 per cent of the control, when measured immediately after the first running fit. Administration of pyridoxine together with SC inhibited the fall. (3) Intracollicular injection of thiosemicarbazide and 4-deoxypyridoxine, other antivitamins B6, also induced running fits.
These results suggest that the running fits by SC injected intracollicularly are induced by the decrease of γ-aminobutyrate due to insufficient vitamin B6 in the superior colliculus.View full abstractDownload PDF (1452K) -
Masanori YASHIRO, Shuichi KIMURA1979 Volume 25 Issue 1 Pages 23-32
Published: 1979
Released on J-STAGE: April 28, 2009
JOURNAL FREE ACCESSThe effects of voluntary exercise on growth and food intake, body composition, organ weight, and fatty acid composition of adipose tissue of mice fed on a 20% casein diet or a 10% casein diet were examined. The weight gain was greater for the 20% casein nonexercise group (20% NE) than that for the 20% casein exercise group (20% E), 10% casein exercise group (10% E) and 10% casein nonexercise group (10% NE). There were no significant differences between the groups except the 20% NE. In 20% E and 10% E, body fats decreased markedly. On the other hand, a very high ratio of protein was present in the body composition of both groups. In the 20% and 10% casein diet groups, food intake was increased by voluntary exercise, but there was no significant difference between 1000 E and 10% NE except occasional periods during these experiments. After 6 weeks of age, 1000 E had a tendency to undertake more voluntary exercise than 20% E, though the difference was not statistically significant. Development of the heart and gastrocnemius muscles was accelerated by voluntary exercise and epididymal fat tissue was markedly decreased.View full abstractDownload PDF (1011K) -
Hiroshi DOI, Noboru KAWAGUCHI, Fumio IBUKI, Masao KANAMORI1979 Volume 25 Issue 1 Pages 33-41
Published: 1979
Released on J-STAGE: April 28, 2009
JOURNAL FREE ACCESSIn order to clarify the function of the carbohydrate moiety of bovine κ-casein, κ-casein components having different carbohydrate contents were prepared by DEAE-cellulose chromatography. Five adsorbed fractions so obtained had an identical peptide chain and contained carbohydrate moieties of increasing size in the order of components P-2, P-3, P-4, P-5 and P-6. The susceptibility of κ-casein components, having different carbohydrate contents, to various proteases was examined. κ-Casein components were subjected to calf rennin [chymosin; EC 3.4.23.4], bovine trypsin [EC 3.4.21.4], α-chymotrypsin [EC 3.4.21.1], pronase [EC 3.4.24.4] and human plasmin [EC 3.4.21.7]. The component containing a larger carbohydrate moiety was less susceptible to hydrolysis than the component containing a smaller carbohydrate moiety. Rennin, trypsin, α-chymotrypsin and pronase hydrolyzed each component with a different reaction rate. On the contrary, human plasmin hydrolyzed component P-2, but did not hydrolyze component P-5. These results indicate that the carbohydrate moiety of κ-casein affected the suscepti-bility of κ-casein components to various proteases.View full abstractDownload PDF (1263K) -
Toshio MITSUNAGA1979 Volume 25 Issue 1 Pages 43-52
Published: 1979
Released on J-STAGE: April 28, 2009
JOURNAL FREE ACCESSTrypsin inhibitors were isolated from wheat germ and two major inhibitors (trypsin inhibitors I and II) were purified by various chromatographies including ion-exchange chromatographies on DEAE-Sephadex and CM-Sephadex as well as gel filtration on Bio-gel and Sephadex. Both inhibitors were polypeptides composed solely of amino acids. In the presence of 1% SDS, inhibitor I showed a single symmetrical sedimentation boundary of 1.6 S and a single band in SDS-gel electrophoresis, but in the absence of SDS, it tended to aggregate. Inhibitor II was found to be homogeneous in gel electrophoresis and velocity sedimentation with or without SDS in the solutions. The molecular weights of inhibitors I and II were approximately 16, 000 and 10, 000, respectively, by SDS-gel electrophoresis. Some other properties of the two inhibitors, including specific inhibitory activities, amino acid compositions and UV spectral properties are presented.View full abstractDownload PDF (2055K) -
Yoshihiro SHIDOJI, Makoto WATANABE, Yasutoshi MUTO1979 Volume 25 Issue 1 Pages 53-57
Published: 1979
Released on J-STAGE: April 28, 2009
JOURNAL FREE ACCESSDownload PDF (542K)
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