Biomedical subjects

Y Sakano

Publications and source records attributed to Y Sakano.

At least 19 recordsLinked to original sources

PubMed1991

Cloning and nucleotide sequence of the gene (citA) encoding a citrate carrier from Salmonella typhimurium.

A cryptic citrate transport gene (citA) from Salmonella typhimurium chromosome was cloned and its nucleotide sequence was determined. The cloned plasmid conferred citrate-utilizing ability on wild-type Escherichia coli, which cannot grow on citrate as the sole source of carbon. The resultant E. coli transformant was able to transport citrate. A 1,302-base-pair open reading frame with a preceding ribosomal binding site was found in the cloned DNA fragment. The 434-amino-acid protein that could be translated from this open reading frame is highly hydrophobic (69% nonpolar amino acid residues), consistent with the fact that the transport protein is an intrinsic membrane protein. The molecular weight of this protein was calculated to be 47,188. The gene sequence determined is highly homologous to those of Cit+ plasmid-mediated citrate transport gene, citA, from E. coli, the chromosomal citA gene from Citrobacter amalonaticus and the chromosomal cit+ gene from Klebsiella pneumoniae. The hydropathy profile of the deduced amino acid sequence suggests that this carrier has 12 hydrophobic segments, which may span the membrane lipid bilayer.

Amino Acid Sequence↗

PubMed1991

Comparison of factor-analyzed Adolescent Reinforcement Survey Schedule (ARSS) responses from Japanese and American adolescents.

The Adolescent Reinforcement Survey Schedule (ARSS) was administered to a sample of male and female late adolescent college students from Japan (N = 500). The responses to the ARSS are factor analyzed using a principal component method. The results of the factor-analyzed ARSS from the Japanese sample are compared and contrasted with the results from a previous study (Holmes et al., 1987) in which ARSS was administered to a sample of American male and female college students (N = 231). Both the American and Japanese samples produced 10 interpretable factors. A recommendation is made to replicate the present study with groups of early and mid-adolescents in each culture in order to study shifts in reinforcers during different periods of adolescent development.

Adolescent↗

PubMed1990

Effects of reduced malto-oligosaccharides on the thermal stability of pullulanase from Bacillus acidopullulyticus.

We investigated the effects of the reduced malto-oligosaccharides, D-glucitol (G1-OH), maltitol (G2-OH), maltotriitol (G3-OH), maltotetraitol (G4-OH), and maltopentaitol (G5-OH) on the thermal stability of Bacillus acidopullulyticus pullulanase (EC 3.2.1.41). The thermal stability depended on the concentration of D-glucitol; after heat treatment for 90 min at 60 degrees in the presence of 0.56, 0.28, 0.14, or 0M G1-OH, the residual activity was 100, 80, 32, and 10% of the control, respectively. Stability increased with the number of glucosyl residues in the alditols added; the effects of G3-OH, G4-OH, and G5-OH on stability were remarkable. Addition of 30% G2-OH, G3-OH, and G4-OH also contributed to the thermal stability of the pullulanase immobilized onto chitosan beads treated with glutaraldehyde. A high concentration of G2-OH stabilized other debranching amylases, Klebsiella pneumoniae pullulanse, Bacillus sectorramus pullulanase, and Pseudomonas amyloderamosa isoamylase (EC 3.2.1.68) under heat treatment for 48 h at 60 degrees, as well as the pullullanase of B. acidopullulyticus.

Amylases↗

PubMed1990

Nonenzymatic glycation alters properties of collagen as a substratum for cells.

Acid-soluble collagen from rat skin was glycated in vitro by incubating with 0.2 M D-ribose at 37 degrees C for several days, and properties of the glycated collagen as a substratum for fibroblasts 3 Y 1 were studied. The cells attached but spread poorly on the glycated collagen as compared with on the untreated collagen. Thymidine incorporation by the cells on the glycated collagen was higher than that by the cells on untreated collagen. These results indicate that the glycation significantly alters properties of collagen as a substratum for cells.

Animals↗

PubMed1989

Cell-adhesive immunoglobulin M in human plasma.

Human plasma contains a cell-adhesive protein that has a structure related to immunoglobulins. This protein was purified by affinity chromatography on an elastin-Sepharose column and by Mono Q anion-exchange chromatography. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis under non-reducing and reducing conditions revealed that this protein is a kind of immunoglobulin M (IgM). Antibodies against the mu chain and against the Fc region of IgM inhibited the adhesion of cells to this protein. Addition of the peptide GRGDS into media inhibited the adhesion, too. These results suggest that this protein is a special subset of IgM having a cell-binding sequence in the Fc region. We propose the name "cell-adhesive immunoglobulin M (CA-IgM)" for this protein. CA-IgM binds to alpha-elastin and laminin suggesting that it may play a role in the interaction between cells and the extracellular matrix.

Animals↗

PubMed1989

[Relapsing polychondritis: report of 4 cases].

Four cases of Relapsing Polychondritis followed in the Hospital do Servidor Publico Estadual de Sao Paulo, since 1985, are reported and discussed. Relapsing Polychondritis, an auto-immune disease that destroys the pinnal and nasal cartilage has been observed occasionally around the world. Since it was first defined and described, in 1923, about 250 cases have been reported.

Adult↗

PubMed1987

Cross-linking of collagen by ascorbate-copper ion systems.

Cross-linking occurred rapidly in collagen when it was treated with ascorbate-copper ion systems. Sodium dodecyl sulfate-polyacrylamide gel electrophoretic patterns of CNBr peptides suggest that in some respects the modifications by the ascorbate-copper ion systems mimicked those that occurred in collagen with aging.

Animals↗

PubMed1985

Neutral oligosaccharides in the urine of a patient with glycogen storage disease type II.

Neutral oligosaccharides were isolated from urine of an adult patient with glycogen storage disease type II, a deficiency of lysosomal acid alpha-glucosidase, by chromatography on columns of activated charcoal, Dowex 50 X 2 and Dowex 1 X 2. Total neutral oligosaccharides in the urine of the patient were increased about 5-fold as compared with those in normal controls. The most accumulated oligosaccharide was separated by Bio-Gel P-2 column chromatography, and finally purified by paper chromatography. Based on various studies, including carbohydrate analysis, chemical ionization mass spectrometry, fast atom bombardment mass spectrometry, degradation by glucoamylase and isopullulanase, and methylation analysis, the structure of this oligosaccharide was deduced to be Glc alpha 1----6Glc alpha 1----4Glc alpha 1----4Glc. This oligosaccharide appears to be accumulated in urine of the patient with acid alpha-glucosidase deficiency as an end product of the hydrolysis of glycogen.

Carbohydrate Sequence↗

PubMed1985