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Volume 26 (1980)
- Issue 6 Pages 521-
- Issue 5 Pages 419-
- Issue 4 Pages 327-
- Issue 3 Pages 189-
- Issue 2 Pages 103-
- Issue 1 Pages 1-
Predecessor
Volume 26, Issue 2
Displaying 1-8 of 8 articles from this issue
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Makoto MINO, Yoshitami KIJIMA, Yasuhiko NISHIDA, Shigeo NAKAGAWA1980 Volume 26 Issue 2 Pages 103-112
Published: 1980
Released on J-STAGE: April 28, 2009
JOURNAL FREE ACCESSThis study is concerned with differences between breast-fed and bottle-fed infants in plasma and red blood cell (RBC)-levels and pattern of tocopherol analogues. Tocopherol levels were determined by High-Performance Liquid Chromatography (HPLC). The results were as follows:
1. In breast-fed infants the plasma contained larger amounts of the alpha and smaller amounts of the gamma form of tocopherol than in bottle-fed infants but the RBC contained the alpha form alone.
2. In the bottle-fed infants the plasma contained the alpha, gamma, and delta forms, but the RBC contained the alpha form alone.
3. In bottle-fed infants plasma alpha-tocopherol levels did not differ significantly from those in breast-fed infants but RBC alpha-tocopherol levels were far lower in the former. In contrast, plasma gammatocopherol levels were significantly higher in bottle-fed infants.
4. Cord blood plasma contained only the alpha and gamma forms with the patterns similar to those in adults. The delta form appeared in the plasma of bottle-fed neonates as early as 3 or 4 days after birth.
5. The transitional-form human milk obtained on the 5th postpartum day contained the alpha and gamma forms alone and resembled adult plasma. On the other hand, commercially available formulas contained all four forms, with the gamma form the highest, alpha and delta forms moderate, and only slight beta.View full abstractDownload PDF (733K) -
Shuichi KIMURA, Yuji FURUKAWA, Jun-ichiro WAKASUGI, Yasuyuki ISHIHARA, ...1980 Volume 26 Issue 2 Pages 113-117
Published: 1980
Released on J-STAGE: April 28, 2009
JOURNAL FREE ACCESSThe inhibition rate of L (-) pantothenate as an antagonist of D (+) pantothenate was discussed from the viewpoint of growth and lipid metabolism. The growth rate of mice given pantothenate-deficient diets containing L (-) pantothenate (300 mg per 100 g diet) was markedly decreased, and such pantothenate-deficient symptoms as “spectacle eyes” appeared. However, it was recovered by the simultaneous addition of D (+)pantothenate. This result suggests that L (-) pantothenate is an antagonist of D (+) pantothenate. The same phenomenon was observed in a rat experiment. The growth of rats given L (-) pantothenate was extremely poor but recovered by the simultaneous addition of D (+) pantothenate. Its complete recovery was seen when the ratio of L (-) pantothenate to D (+) pantothenate reached 100:1. The same tendencies were observed in the liver levels of total lipid, total cholesterol and triglyceride, and also in the lipoperoxide values. This experiment suggests that the inhibition rate of L (-) pantothenate to D (+)pantothenate in animals is similar to that of DL-ω-methyl pantothenate.View full abstractDownload PDF (382K) -
Fumio IBUKI, Makoto KOTARU, Akihiko KATSURADA, Toshio ASAO, Misao TASH ...1980 Volume 26 Issue 2 Pages 119-126
Published: 1980
Released on J-STAGE: April 28, 2009
JOURNAL FREE ACCESSThe purified trypsin inhibitor from eggplant (Solanum melongena, L.) has an Arg-X bond in the reactive site which is selectively cleaved by limited hydrolysis with a catalytic amount of bovine trypsin. So-called trypsin-modified inhibitor was separated from the native one by QAE-Sephadex A-25 chromatography. After the cleavage of disulfide bonds of isolated modified inhibitor by means of reduction and Scarboxymethylation, two fragments (F-I and F-II) were obtained by gel filtration on Sephadex G-25. F-I and F-II were composed of 44 and 14 amino acid residues, respectively. The sum of both coincided with that of the native inhibitor. The N-terminal of F-I was blocked and the Cterminal was arginine. In F-II, the N-terminal was identified as asparagine and the C-terminal as serine. No N-terminal amino acid could be detected in the native inhibitor, as described in our previous paper (7). Therefore, it is concluded that the reactive site of eggplant trypsin inhibitor is an arginylasparagine bond located between residues 44 and 45.View full abstractDownload PDF (1284K) -
Nanaya TAMAKI, Sachiko MORIOKA, Tatsuhiko IKEDA, Mitsuko HARADA, Takao ...1980 Volume 26 Issue 2 Pages 127-139
Published: 1980
Released on J-STAGE: April 28, 2009
JOURNAL FREE ACCESSThe biosynthesis and destruction of anserine and carnosine in the rat were investigated in vivo using radioactive β-alanine, histidine and methylhistidine. In the normal rat, the incorporation of 14C-histidine and 14C-β-alanine into carnosine was found to proceed at significant rates, but their incorporation into anserine was hardly detectable. Radioactive anserine arising from 3H-Nπ-methylhistidine was detected in gastrocnemius muscle of the rat pretreated with β-alanine. Neither anserine nor carnosine biosynthesis was found in liver, but was found in gastrocnemius muscle. At 8 hr after the administration of a single dose of 14C-histidine or 14C-β-alanine, the incorporation of radioactivity into carnosine attained a plateau, and then maintained the level for the investigated period. Incorporation of 14C-histidine into carnosine was increased about 2-fold when rats were injected in advance with f-alanine. The half-lives of histidine and β-alanine were 0.67 and 0.41 hr in liver, and 3.6 and 2.3 hr in gastrocnemius muscle, respectively. β-Alanine and histidine in rat gastrocnemius muscle disappeared at the rates of 39 and 29 nmol/wet tissue (g)/hr, respectively. The half-life of carnosine, as was determined from the decrease in carnosine contents in the gastrocnemius muscle of a rat fed a histidine-free diet, was 29 days. The rate constant of carnosine biosynthesis in rat gastrocnemius muscle was 0.321 μmol/DNA (mg)/day, that is, 0.286 μmol/wet tissue (g)/day.View full abstractDownload PDF (1217K) -
Sada OHGURI1980 Volume 26 Issue 2 Pages 141-160
Published: 1980
Released on J-STAGE: April 28, 2009
JOURNAL FREE ACCESSThe effects of an excess intake of leucine, for a short period (3 to 4 weeks) and a long period (12 weeks), on growth and excretion of tryptophan and niacin metabolites in rats were studied.
Excess intake of leucine (4 or 5%) for a short period did not affect increase in body weight or organ weight (liver, kidney and heart) compared with those of rats fed the control diet. Excess intake of leucine for a long period resulted in a decrease in body weight, and an increase in the relative weight of the liver and kidney. Urinary excretions of N1-methyl nicotinamide (N-MNA), N1-methyl-2-pyridone-5-carboxamide (2Py), niacin, quinolinic acid and 5-hydroxyindole acetic acid did not differ in rats fed an excess-leucine diet and rats fed a control diet. In niacin deficiency, the excretions of N-MNA, 2-Py and NiA decreased. Excess leucine intake increased the plasma levels of leucine and alanine and decreased those of valine, isoleucine, tryptophan and cystine.
Excess leucine intake decreased the levels of valine, isoleucine, methionine and leucine in the liver, but these changes were not observed in niacindeficient rats. Changes in the levels of nicotinamide mononucleotide (NMN), nicotinamide adenine dinucleotide (NAD), nicotinamide adenine dinucleotide phosphate (NADP) in erythrocytes, suggested to occur in pellagra, were not observed. These findings do not support the idea that an excess intake of leucine results in changes in metabolism similar to those observed in pellagra.View full abstractDownload PDF (1605K) -
Sueko SAGAWA, Keizo SHIRAKI1980 Volume 26 Issue 2 Pages 161-169
Published: 1980
Released on J-STAGE: April 28, 2009
JOURNAL FREE ACCESSThe relation of membrane lipids and osmotic fragility of red cells of human and rat were studied in vitro by repletion and depletion of cell cholesterol. A decrease in the red cell cholesterol corresponded to an increase in osmotic fragility. Conversely, a repletion of red cell cholesterol decreased the osmotic fragility, but the procedure did not significantly change the phospholipid contents of red cells.
Accordingly, osmotic fragility of the red cells correlated highly with the cholesterol content of the cell membrane (r=-0, 944, p<0.001) and with the molar ratio of cholesterol to phospholipid in the red cells (r=-0.887, p<0.001). Red cells incubated with plasma had decreased membrane cholesterol and increased osmotic fragility, but the change was prevented by the inactivation of lecithin cholesterol acyltransferase (LCAT) in the plasma.
The above results confirm that membrane cholesterol stabilizes human and rat red cells in vitro as well as in vivo, and the content of red cell cholesterol is regulated by the exchange of plasma free cholesterol in vitro. LCAT activity in the plasma is an influential factor in controlling the cholesterol content of red cells.View full abstractDownload PDF (777K) -
Kazuhiko YAMADA, Norimasa HOSOYA, Setsuko NODA, Sachiko MORIUCHI1980 Volume 26 Issue 2 Pages 171-182
Published: 1980
Released on J-STAGE: April 28, 2009
JOURNAL FREE ACCESSAppearance of immunoreactive sucrase-isomaltase complex was observed in rat small intestine during postnatal development and maturation along the villus-crypt axis by single radial immunodiffusion. The immunoreactive sucrase-isomaltase complex in brush-border membrane increased in parallel with enzyme activities until weaning. After weaning, higher amounts of the immunoreactive enzyme proteins were found as compared with their activities. On the other hand, during cell maturation in adult rat jejunum, the immunoreactive enzyme proteins increased with the activities of sucrase-isomaltase complex. However, a significant amount of the immunoreactive enzyme proteins was observed in the crypt cells with low enzyme activities. Chromatographic profiles on Sephadex G-200 column of the sucrase-isomaltase complex in the upper villus and crypt cells did not change.
From these results, it is suggested that the appearance of sucrase and isomaltase activities until weaning is ascribed to the synthesis of an active sucrase-isomaltase complex or the synthesis of an inactive proenzyme followed by rapid conversion to active enzyme, and during cell maturation, it is caused by the synthesis of the inactive proenzyme in the crypt cells followed by its activation in the villus cells.View full abstractDownload PDF (1951K) -
Yoshihiro SHIDOJI, Makoto WATANABE, Tsuneyuki OKU, Yasutoshi MUTO, Nor ...1980 Volume 26 Issue 2 Pages 183-188
Published: 1980
Released on J-STAGE: April 28, 2009
JOURNAL FREE ACCESSThe inhibitory effects of β-sitosterol on intestinal cholesterol absorption were studied by means of a dual isotope plasma ratio method (in vivo), which is a new technique for the measurement of cholesterol absorption, as well as a ligated-loop method (in situ). The results obtained were as follows:
1. The absorption of β-sitosterol itself was significantly less than cholesterol. Cholesterol was selectively absorbed from rat intestine.
2. When 100 to 1, 000μg of β-sitosterol were added to the dose solution containing 10μg of cholesterol, cholesterol absorption by the in vivo experiment decreased with the increase of additional β-sitosterol.
3. A similar inhibitory effect of β-sitosterol was observed by the in situ ligated-loop method.
These results suggest that β-sitosterol actually inhibits cholesterol absorption in the physiological state of an animal.View full abstractDownload PDF (662K)
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