UDP-GalNAc : GalNAc-mucin α-N-acetylgalactosamine transferase activity in human intestinal cancerous tissues

GalNAc transferase activities of 6 human intestinal cancerous tissues were examined using bovine submaxillary gland mucin and its desialylated derivative, asialomucin, as acceptors. A Triton X-100 extract of these tissues was used as an enzyme source. All the tissues examined had GalNAc transferase that catalyzes the transfer of GalNAc from UDP-GalNAc to serine or threonine residues of the polypeptide chain. One of 6 specimens showed in addition UDP-GalNAc:GalNAc-mucin α-GalNAc transferase activity, synthesizing a disaccharide unit, GalNAcα→ GalNAc, when asialomucin was used as an acceptor. This carbohydrate structure was deduced on the basis of results of gel filtration, exoglycosidase digestion, and high-voltage paper electrophoresis.GalNAc transferaseHuman intestinal cancerous tissueBovine submaxillary gland mucin O-Glycosidically linked sugar chain     

Cloning of the Escherichia coli gene for the stringent starvation protein

Summary In order to clone the Escherichia coli gene for the stringent starvation protein (SSP), we determined its N-terminal sequence as well as the sequence of two peptide fragments obtained by cyanogen bromide cleavage of the protein. We then chemically synthesized four sets of oligodeoxyribonucleotide mixtures that represented possible codon combinations for parts of these amino acid sequences. The synthetic oligonucleotides were labelled with ³²P at their 5-termini and used as hybridization probes to detect DNA fragments containing the complementary sequences. Genomic Southern hybridization of E. coli chromosomal DNA gave up to ten DNA fragments hybridizing with each probe but only a few hybridized with two or more of the probes. The latter fragments were coloned in pBR322. By determining partial base sequences with a rapid method and examining proteins encoded by the DNA fragments, we were able to show that we had isolated a clone containing the complete SSP structural gene.Abbreviations SSP stringent starvation protein - PTH phenylthiohydantoin     

Flavonoid glycosides of the roots of Glycyrrhiza uralensis

The structure of a flavanone glycoside from the roots of Glycyrrhiza uralensis has been confirmed as 4′-O-[β-d-apio-d-furanosyl-(1 → 2)-β-d-glucopyranosyl]liquiritigenin. In addition, two known flavonoid glucosides, ononin (a minor component) and liquiritin (a major component), were isolated from the same extract.     

In vitro growth of adult amphibian (Xenopus laevis) hepatocytes and characterization of hepatocyte-proliferating activity in homologous serum

Adult frog (Xenopus laevis) hepatocytes were found to proliferate in a culture medium containing adult homologous serum. Insulin and dexamethasone were required for a net proliferation of hepatocytes. Dose-response analysis showed that a low concentration of serum (greater than or equal to 0.5%) was enough to induce DNA synthesis and mitosis, but a higher concentration (5%) caused certain necrotic changes. Under optimal conditions, there was a two- to threefold increase in nuclei per culture 10 days after serum treatment. Heterologous sera (fetal bovine, calf and chick) showed less proliferative activity. Based on our results, hepatocyte-proliferating activity in adult frog serum is considered to be heat-unstable and acidic protein(s). Thus, adult frog serum may contain hepatopoietin possibly different from well-known growth factors.     

Stability enhancement and circular dichroism spectral anomaly as an indication of non-covalent interactions in histidine- and tyrosine-containing ternary copper(II)—amino acid systems

Visible absorption and CD spectral and potentiometric studies on the His- and Tyr-containing ternary copper(II) complexes Cu(A)(L-B), where A refers to L-His, D-His, or L-Tyr and B to Lys, Tyr, Trp, Phe, Ala, Val, Arg, Glu, Asn, Gln, Ser, or Thr, were made to study ligand-ligand interactions in the complexes. While the CD spectral magnitudes in the d—d region are additive in the absence of side chain interactions and can be estimated from the magnitudes for the ternary systems involving DL-A or DL-B, deviation from the additivity was observed for Cu(L-His)(L-B) (B = LysH, Tyr, Trp, or Phe) and Cu(L-Tyr)(L-Trp). From the stability constants determined at 25 °C and I = 0.1 M (KNO₃), the equilibrium constants, K, for the following hypothetical equilibria were calculated to be large (0.14–0.60) for formation of Cu(L-/D-His)(L-B)(B = Tyr or Trp) and Cu(D-His)(L-Phe) with Cu(en)(L-Ala) as standard: $Cu(A)(L?Ala)+Cu(en)(L?b)\stackrel{K}{?}Cu(A)(L?B)+Cu(en)(L?Ala)$ The positive values indicate the stabilization due to the stacking between the imidazole ring of His and the aromatic side chain of L-B. Solvent dependence of the CD spectra for Cu(L-His)(L-LysH) and Cu(L-His) L-Trp) further supported the existence of the intramolecular electrostatic and hydrophobic interactions.     

Axial ligation of nitrogenous bases to five-coordinate chloro-meso-tetraphenylporphyrinatochromium(III)

The axial ligations of nitrogenous bases to the five-coordinate chloro-meso-tetraphenylporphyrinatochromium(III) [Cr(III)(TPP)(Cl)] were studied in a non-coordinating solvent, dichloromethane (CH₂Cl₂), by spectrophotometric methods. A correlation exists between log K for the axial ligation:

and pK_a for the N-donor ligand. This correlation suggests that ligand to metal σ bonding contributes to the complex formation, rather than does metal to ligand π back-donation.     

The Escherichia coli cytochrome b556 gene, cybA, is assignable as sdhC in the succinate dehydrogenase gene cluster

Abstract The cytochrome b556 -deficient mutant Escherichia coli K12 strain TK3D11 [7] could not grow with succinate as the sole carbon source, but could grow well on dl -lactate. This finding suggested that cytochrome b556 is primarily responsible for oxidative metabolism and utilization of succinate. 24 Amino acid residues at the amino-terminal of purified cytochrome b556 were determined. This sequence coincided completely with amino acid residues 4 to 27, predicted from the DNA sequence of the sdhC gene, one of the unassigned open reading frames of the sdh gene cluster recently reported by Wood et al. [16]. Based on these and other results, we concluded that cybA , the gene for cytochrome b556 , is assignable as sdhC .     

On the sexual reproduction ofDictyosiphon foeniculaceus (Phaeophyceae,Dictyosiphonales)

Dictyosiphon foeniculaceus from Sweden and Newfoundland was studied in laboratory culture. Zoids from unilocular sporangia developed into dioecious microscopic filamentous gametophytes which produced uniseriate plurilocular gametangia in low temperatures (0 to 8 °C). Zygotes and unfused isogametes gave rise to filamentous protonemata on which parenchymatous macroscopic sporophytes were formed. Isolates from Sweden and Newfoundland were interfertile. Although formed in culture, genetically unisexual sporophytes were not detected in nature. Female gametes ofD. foeniculaceus produced a sexual pheromone. It was identified as finavarrene, which is also known as the sperm attractant inAscophyllum nodosum.     

Chromosomal location of the Escherichia coli cytochrome b556 gene, cybA

Summary The amounts of cytochrome b556 in the cytoplasmic membranes of several Escherichia coli K12 strains having F-prime factors and a lambda transducing phage were determined. The amount was amplified about two-fold in strains having F100-12 and F152, but not in strains having F100-11, F8 and psu ⁺ 2glnS ⁺. The strain TK3D11, which lacks the kdp-gltA region (deletion D-01) of the E. coli chromosome, did not synthesize cytochrome b556 at all. From these results, the gene cybA encoding cytochrome b556 was located in the kdp-gltA region.In the cytochrome b556-deficient mutant, a novel b type cytochrome, cytochrome b561 which is a product of the gene cybB, was identified. It seems to function as a physiological electron transferring cytochrome in place of cytochrome b556 in this mutant.Abbeviations HPLC high performance liquid chromatography - EDTA ethylenediamine tetraacetic acid - SDS sodium dodecyl sulfate - NADH reduced form of nicotinamide adenine dinucleotide