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M Taketoshi

Publications and source records attributed to M Taketoshi.

11 recordsLinked to original sources

Haemagglutinating activities of oral strains of Streptococcus milleri group.

Of a total 148 strains of Streptococcus milleri group, 66 agglutinated sheep erythrocytes. The haemagglutinating strains were confined to serotypes g, h, i, j or were untypeable, and had no Lancefield group antigens (A to G and K), all of which have been shown to belong to Streptococcus intermedius. Cell surface hydrophobicity did not significantly differ even between the agglutinating and non-agglutinating S. intermedius strains. The haemagglutinating activity of strain 0813-1 (serotype i) was partially sensitive to heat (100 degrees C, 30 min) or trypsin (1 mg/ml, 30 min) treatment, but completely lost after the heat and subsequent trypsin treatments. Only L-arginine, L-lysine (100 mM), mucin, and fetuin (1 mg/ml) partially inhibited the haemagglutination with native bacterial cells but completely inhibited that with heated cells, whereas none was inhibitory in the reaction with trypsin-treated cells. The results suggest that at least two haemagglutinins are involved in the agglutination of the S. intermedius strain and that the heat-stable but trypsin-sensitive haemagglutinin recognizes the receptors on the erythrocyte surface which contain L-arginine and L-lysine at the reactive site.

Amino Acids↗

Enzymatic differentiation and biochemical and serological characteristics of the clinical isolates of Streptococcus angiosus, S. intermedius and S. constellatus.

Of the 29 'Streptococcus milleri' strains tested, all thirteen Streptococcus intermedius (DNA homology group 2) strains but none of the thirteen Streptococcus anginosus (group 1) strains produced beta-N-acetylglucosaminidase, beta-N-acetylgalactosaminidase, alpha-N-acetylneuraminidase, beta-galactosidase, alpha-glucosidase, and hyaluronidase. The three Streptococcus constellatus (group 3) strains produced only the latter two. Glycosidase production divided 274 clinical isolates into 103 S. anginosus, 101 S. intermedius, and 70 S. constellatus strains. Generally, strains of S. anginosus and S. intermedius were non-beta-haemolytic. API II and biotype Ia (lactose positive), but the former contained almost all API III strains and belonged to Lancefield group A/serotype a (A/a), -/b, C/c, -/d, -/e, F/f or G/k, and the latter included most of biotype IId (lactose negative) and serovar -/g, -/h, -/i or -/j. S constellatus strains were beta-, alpha- or gamma-haemolytic, of API I or II but mostly biotype Ib (lactose negative), and of F/- or -/b. S. intermedius was a major member of the oral isolates. Non-oral isolates were virtually all S. anginosus (mainly urogenital isolates) or S. constellatus (the other systemic isolates).

Adult↗

Deoxyribonucleic acid relatedness and phenotypic characteristics of oral Streptococcus milleri strains.

Strains of oral Streptococcus milleri group were compared with the type strains of Streptococcus anginosus, S. intermedius, and S. constellatus by DNA-DNA hybridization at 60 degrees C. Of the 29 strains tested, twelve, twelve, and two strains were closely related to S. anginosus ATCC 33397T, S. intermedius ATCC 27335T, and S. constellatus ATCC 27823T, respectively. Generally, the strains classified in the S. anginosus group in DNA homology were non-beta-haemolytic and belonged to API S. milleri II and biotype I (lactose fermenting), whereas the strains of S. constellatus group were beta-haemolytic and belonged to API S. milleri I and biotype II (lactose non-fermenting). The strains of the S. intermedius group were all non-beta-haemolytic and belonged to API S. milleri II and mostly biotype II (lactose fermenting). Furthermore, all except one strain of the S. anginosus group were Lancefield group A/serotype a (A/a), ungroupable/serotype b (-/b), C/c, -/d, -/e, F/f or G/k, whereas those of the S. constellatus group were F/-. The strains of the S. intermedius group were -/g, -/h, -/i, -/j, or -/-.

DNA Probes↗

Molecular cloning of guinea-pig aromatic-L-amino acid decarboxylase cDNA.

Guinea-pig aromatic-L-amino acid decarboxylase (DOPA decarboxylase, DDC), but not rat DDC, reacts with the antibody against rat histidine decarboxylase (HDC). For determination of the molecular reaction for this cross-reactivity, a cDNA clone of guinea-pig DDC was isolated. Guinea-pig DDC consists of 480 amino acids and its molecular weight is 54,148. The sequence identify of guinea-pig DDC with rat DDC is 86%. Guinea-pig DDC has a region showing 100% sequence identity with rat HDC, but only 67% sequence identity with rat DDC, suggesting that this region is related with the cross-reactivity of guinea-pig DDC and anti-rat HDC antibody.

Amino Acid Sequence↗

Molecular cloning and sequencing of a cDNA of rat dopa decarboxylase: partial amino acid homologies with other enzymes synthesizing catecholamines.

Dopa decarboxylase (DDC; aromatic-L-amino-acid decarboxylase; aromatic-L-amino-acid carboxylase, EC 4.1.1.28) was purified from rat liver and its partial sequence was determined. Synthetic oligonucleotides were used to construct and screen rat liver cDNA libraries, and three clones were isolated and sequenced. The 2 kilobases of DDC cDNA cloned consisted of a 5'-noncoding segment of 78 nucleotides, a coding region of 1440 nucleotides, and a 3'-noncoding region of 438 nucleotides. The encoded protein of 480 amino acid residues had a molecular weight of 54,000. A special feature of the primary structure of rat DDC was a repeating structure consisting of 29 amino acid residues. A sequence of 58 amino acid residues, including this repeating structure of rat DDC, was found to show homologies with those of rat tyrosine hydroxylase, human dopamine beta-hydroxylase, and bovine phenylethanolamine N-methyltransferase, other mammalian enzymes that synthesize catecholamines. These results indicate that catecholamine biosynthetic enzymes are structurally related and suggest that their homologous domains are important for catechol-protein interactions.

Amino Acid Sequence↗

Induction of cytosolic aspartate aminotransferase by glucagon in primary cultured rat hepatocytes.

The activity and the mRNA content of cytosolic aspartate aminotransferase (EC 2.6.1.1) were examined in cultured rat hepatocytes. Addition of glucagon (1 x 10(-7) M) in the presence of dexamethasone (1 x 10(-7) M) caused about 2-fold increase in the activity and mRNA content. Dibutyryl cAMP (1 x 10(-4) M) could replace glucagon for this effect. Maximal induction of cytosolic aspartate aminotransferase mRNA was observed 8 h after their additions. Insulin (1 x 10(-7) M) did not inhibit the enzyme induction by glucagon or dibutyryl cAMP. These results suggest that the cytosolic aspartate aminotransferase gene is regulated by cAMP, and not by insulin.

Animals↗

Rat cytosolic aspartate aminotransferase: molecular cloning of cDNA and expression in Escherichia coli.

cDNA clones for rat cytosolic aspartate aminotransferase (cAspAT, L-aspartate:2-oxoglutarate aminotransferase) [EC 2.6.1.1] were isolated from a rat cDNA library, and the primary structure of the gene for cAspAT was deduced from its cDNA sequence. Rat cAspAT consists of 412 amino acids and its molecular weight is 46,295. The deduced amino acid sequence of rat cAspAT was compared with the sequences of AspATs from other species. The degree of sequence identities of rat/mouse cAspAT, rat/pig cAspAT, rat/chicken cAspAT, rat/pig mAspAT, and rat/Escherichia coli AspAT were 97.1, 89.6, 81.7, 48.1, and 41.2%, respectively. A coding region of rat cAspAT cDNA was inserted into E. coli expression vector pUC9, and enzymatically active cAspAT was expressed as a beta-galactosidase-cAspAT hybrid protein. This hybrid protein represented about 18% of the soluble proteins in E. coli and its kinetic properties were comparable with those of cAspAT preparations purified from rat liver.

Amino Acid Sequence↗

Rat cytosolic aspartate aminotransferase: regulation of its mRNA and contribution to gluconeogenesis.

Induction of cytosolic aspartate aminotransferase (cAspAT) was observed in rat liver on administration of a high-protein diet, or glucagon and during fasting. The enzyme activity in the liver of rats given 80% protein diet or glucagon injection during starvation increased to 2- to 2.4-fold that in the liver of rats maintained on 20% protein diet, with about 2-fold increases in the levels of hybridizable cAspAT mRNA, measured by blot analysis using the cloned rat cAspAT cDNA as a probe. No increase in the enzyme was detected in kidney, heart, brain, or skeletal muscle. The activity of mitochondrial aspartate aminotransferase (mAspAT) did not increase. Induction of cAspAT was observed when glucose metabolism tended toward gluconeogenesis. The physiological function of the induction of cAspAT is considered to be to increase the supply of oxaloacetate as a substrate for cytosolic phosphoenolpyruvate carboxykinase (PEPCK) [EC 4.1.1.32] for gluconeogenesis.

Animals↗

Molecular cloning of rat mitochondrial glutamic oxaloacetic transaminase mRNA and regulation of its expression in regenerating liver.

cDNA clones for rat mitochondrial glutamic oxaloacetic transaminase (mGOT) have been isolated from a rat liver cDNA library. One of the clones, designated p501, contained a cDNA insert of 1.4 kilobase pairs in length and hybridized to a mRNA of 2.4 kilobases from rat liver. We measured mGOT mRNA content in a regenerating rat liver. In a regenerating rat liver, mGOT activity was increased and reached maximum (170% of control activity) at about 48 h following the operation. Using the cDNA of mGOT, it was revealed that the increase of mGOT in the regenerating rat liver depended on its mRNA content.

Animals↗

The relation between Ames test data and electronic structure for a series of benzidine derivatives investigated by using cluster analysis.

The dose-response curves of benzidine derivatives calculated from Ames test data were analyzed by combining the least-squares method with cluster analysis. The calculations of the electronic structures of various benzidine derivatives have at the same time been performed by using the CNDO/2 method. The cluster analysis was carried out on various parameters concerning the electronic structure, such as total electron density, frontier electron density, the energy level of HOMO (highest occupied molecular orbital), and so on. It was found that the total electron density on the nitrogen atom gives a similar pattern of classification to that for mutagenic compounds in cluster analysis. In other words, it may be inferred that the nitrogen atoms of the benzidine derivatives play an important role in the metabolic activation of the compounds. Consequently, cluster analysis with a parameter of electronic structure should be a useful initial screening procedure for various analogous mutagenic compounds as well as carcinogenic compounds.

Benzidines↗