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Biomedical subjects

H Chiba

Publications and source records attributed to H Chiba.

At least 253 records · Page 14Linked to original sources
PubMed1983

Quality deterioration of winged bean during storage.

Seeds of winged bean (Psophocarpus tetragonolobus) were stored under four different sets of conditions; 65% relative humidity (RH) at 5 degrees C, 35% RH at 37 degrees C, 65% RH at 37 degrees C, and 85% RH at 37 degrees C. After storage for three and five months, samples were taken out to explore quality changes during storage. The germination capacity decreased during storage at high temperatures. Although little change was found in content in extractable oil, a decrease in the iodine value and an increase in the acid value and in the TBA value were significant during storage at high temperature and high moisture, indicating deterioration of oil. Aldehyde in defatted bean extract increased under all conditions for storage. Protein extractability was greatly reduced at 36 degrees C and 85% RH, while no reduction was observed at other conditions.

Fabaceae↗
PubMed1981

Purification and characterization of four components of rat caseins.

Rat casein components (C1-, C3A-, C3B- and C4-casein) were extensively purified from rat milk, and the properties of these proteins were compared with those of other caseins including rat C2-casein. C1-casein was precipitated by a low concentration of CaCl2 (1.5 mM). Both C3A- and C3B-casein were less sensitive to Ca2+ than were C1- and C2-casein, and the presence of 20 mM CaCl2 was required at 37 degrees C for their precipitation. C4-casein was absolutely insensitive to Ca2+. This protein exhibited the ability to stabilize all of the other rat casein components against Ca2+-dependent precipitation. In addition, C4-casein contained sialic acid, galactose and N-acetylgalactosamine. Therefore, C4-casein appears to be a bovine kappa-casein-like protein.

Amino Acids↗
PubMed1981

Synthesis of 2,3-bisphosphoglycerate synthase in erythroid cells.

Antiserum prepared from a rabbit which was immunized with human erythrocyte glycerate-2,3-P2 synthase was found to react with glycerate-2,3-P2 synthase in rabbit erythroid cells. By using this antiserum, it was proved that the specific activity of this enzyme was unchanged during the development of the rabbit erythroid cells. This leads us to conclude that the increased activity of glycerate-2,3-P2 synthase in developing erythroid cells (Narita, H., Ikura, K., Yanagawa, S., Sasaki, R., Chiba, H., Saimyoji, H., and Kumagai, N. (1980) J. Biol. Chem. 255, 5230-5235) is due to the accumulation of enzyme protein. There is at least a 16-fold increase in the level of this protein during development from bone marrow erythroid cells to erythrocytes. The synthesis of glycerate-2,3-P2 synthase was shown to occur in rabbit reticulocytes and bone marrow erythroid cells. These cells were incubated for protein synthesis and the protein synthesized was precipitated with the anti-glycerate-2,3-P2 synthase antiserum and separated on sodium dodecyl sulfate-polyacrylamide gels. The immunoprecipitated product was shown to produce fragments of the same molecular weight after digestion with V8 protease as did the pure glycerate-2,3-P2 synthase. The proportion of glycerate-2,3-P2 synthase synthesis in reticulocytes (0.04% of total protein synthesis) was comparable to the level of this protein in the cells (0.07% of the total protein).

Animals↗
PubMed1981

Purification and properties of a major casein component of rat milk.

A casein component (C2-casein) was purified by ion-exchange and gel filtration chromatography from rat milk, and the properties of this protein were examined. The molecular weight of C2-casein, as determined by Sepharose 4B gel filtration in 6 M guanidine hydrochloride, was 34 000 +/- 1000. The average hydrophobicity calculated from the amino acid composition showed that C2-casein is a rather hydrophilic protein. The alpha-helix content obtained from optical rotatory dispersion experiments was about 12%. In ultracentrifugation analyses, monomer and polymer peaks of C2-casein were both seen, and the monomer-to-polymer ratio was not affected by changing temperature conditions. C2-casein was precipitated by the presence of 2.5 mM CaCl2, and the precipitability was greatly decreased by the dephosphorylation of the protein. C2-casein was stabilized from Ca2+-dependent precipitation by the addition of another rat casein component (C3-casein) or of bovine kappa-casein.

Amino Acids↗
PubMed1981

Changes in the enzymes related to 2,3-bisphosphoglycerate metabolism in developing erythroid cells.

Measurements of glycerate-2,3-P2 and hemoglobin in the developing erythroid cells indicated that the glycerate-2,3-P2 level rose during erythroid differentiation in a linear relationship to the hemoglobin level, suggesting the presence of regulation to accumulate both substances synchronously. The accumulation of glycerate-2,3-P2 was found to be primarily attributable to the increase in glycerate-2,3-P2 synthase activity. The activities of phosphofructokinase and pyruvate kinase changed so as to be favourable for glycerate-2,3-P2 accumulation. The increase in glycerate-2,3-P2 synthase activity was shown to be caused by an increase in the enzyme protein. Synthesis of glycerate-2,3-P2 synthase protein was proved in bone marrow erythroid cells and in reticulocytes.

2,3-Diphosphoglycerate↗
PubMed1981

Localization of bovine liver aldehyde dehydrogenase isozymes and their immunological properties.

Evidence supporting the existence of three aldehyde dehydrogenases in bovine liver has been confirmed and the immunological properties of these isozymes have been compared. 1. The cytoplasmic and mitochondrial aldehyde dehydrogenases were distinguished in size by subjecting the bovine liver crude extract to Sephadex G-150 chromatography. The molecular weight of the cytoplasmic aldehyde dehydrogenase was determined to be 230,000 daltons, larger than the mitochondrial enzyme by approximately 15,000 daltons. 2. Submitochondrial fractionation indicated that the mitochondrial aldehyde dehydrogenase was located in the intermembrane space. 3. Anti-mitochondrial aldehyde dehydrogenase antibody from rabbit gave an immunoreaction line not only with the mitochondrial enzyme but also with the cytoplasmic enzyme, and inhibited the activity of both enzymes. The anti-cytoplasmic aldehyde dehydrogenase antibody reacted with the cytoplasmic enzyme but had no effect on the mitochondrial enzyme. Neither antibody reacted with the microsomal aldehyde dehydrogenase solubilized with sodium deoxycholate.

Acetaldehyde↗
PubMed1980

2,3-Bisphosphoglycerate in developing rabbit erythroid cells.

Rabbits were made anemic to different extents by phenylhydrazine injections so as to vary the developmental stages of the erythroid cells in their peripheral blood and bone marrow. It was found that the more severe the anemia, the lower the concentration of glycerate-2,3-P2 in the bone marrow cells and in the circulating erythroid cells. The glycerate-2,3-P2 level was shown to rise during erythroid differentiation in a linear relationship to the hemoglobin level, corresponding to the equation Y = 0.03x + 0.29, where y is the concentration of glycerate-2,3-P2 (micromoles per ml packed cells) and x is the concentration of hemoglobin (milligrams per packed cells). The bone marrow cells were fractionated on a size (i.e. maturity) basis and enzyme activities in the fractionated cells were measured. The accumulation of glycerate-2,3-P2 was found to be primarily attributable to the increase in glycerate-2,3-P2 synthase activity. Glycerate-2,3-P2 phosphatase and phosphofructokinase increased as the cells matured from the polychromatic stages to become reticulocytes while pyruvate kinase and phosphoglyceromutase decreased. The changes in phosphofructokinase and pyruvate kinase appear to be advantageous for glycerate-2,3-P2 accumulation. The two enzyme activities directly responsible for the synthesis and the breakdown of glycerate-2,3-P2 are probably manifested by a single protein, glycerate-2,3-P2 synthase-phosphatase.

Anemia↗