Role of magnesium ion on the interaction between chromomycin A3 and deoxyribonucleic acid

Abstract is not available.

Effect of the antitumor antibiotic chromomycin A3 on the humoral immune response in rats

Chromomycin A3 (250 mug/kg) suppressed the humoral immune response in rats against sheep erythrocytes when administered 48 h or later after antigenic stimulus. The antibiotic at this dose enhanced immunity when given along with or before antigen administration. The natural heterohemagglutinin levels in rabbits and guinea pigs were not affected by the antibiotic (10 mug/kg per day x 7).

Mode of action of antitumour antibiotics: Spectrophotometric studies on the interaction of chromomycin A3 with DNA and chromatin of normal and neoplastic tissue

The binding of chromomycin A3, an antitumour antibiotic, to various DNA and chromatin isolated from mouse and rat liver, mouse fibrosarcoma and Yoshida ascites sarcoma cells was studied spectrophotometrically at 29°C in 10−2 M Tris-HCl buffer, pH 8.0, containing small amounts of MgCl2 (4.5 · 10−5−25 · 10−5 M). An isobestic point at 415 nm was observed when chromomycin A3 was gradually titrated with Image and its spectrum shifted towards higher wavelength. The rates and extent of these spectral changes were found to be dependent on the concentration of Mg2+. The change in absorbance at 440 nm was used to calculate apparent binding constant (Ka p M−1) and sites per nucleotide (n) from Scatchard plots for various DNA and chromatins. As expected, values of n for chromatin (0.06–0.10) were found to be lower than that found for corresponding DNA (0.10–0.15). Apparently no such correlation exists between binding constants (Ka p M−1 · 10−4) of DNA (6.4–11.2) and of chromatin (3.1–8.3), but Ka p M−1 of chromatin isolated from mouse fibrosarcoma and Yoshida ascites sarcoma are 1.5–3 times higher than that found for mouse and rat liver chromatin. These differences may be taken to indicate structural difference in nucleoprotein complexes caused by neoplasia. The relevance of this finding to tumour suppressive action of chromomycin A3 is discussed.

Formation and structure of composite coating of HDA and micro-plasma oxidation on A3 steel

Composite coatings were obtained on A3 steel by hot dipping aluminum(HDA) at 720 ℃ for 6 min and micro-plasma oxidation(MPO) in alkali electrolyte. The surface morphology, element distribution and interface structure of composite coatings were studied by means of XRD, SEM and EDS. The results show that the composite coatings obtained through HDA/MPO on A3 steel consist of four layers. From the surface to the substrate, the layer is loose Al2O3 ceramic, compact Al2O3 ceramic, Al and FeAl intermetallic compound layer in turn. The adhesions among all the layers are strengthened because the ceramic layer formed at the Al surface originally, FeAl intermetallic compound layer and substrate are combined in metallurgical form through mutual diffusion during HDA process.Initial experiment results disclose that the anti-corrosion performance and wear resistance of composite coating are obviously improved through HDA/MPO treatment.

Formation and Structure of Composite Coating of HAD and Micro-Plasma Oxidation on A3 Steel

Composite coatings were obtained on A3 steel by hot dipping aluminum(HAD) at 720 degreesC for 6 min and micro-plasma oxidation (MPO) in alkali electrolyte. The surface morphology, element distribution and interface structure of composite coatings were studied by means of XRD, SEM and EDS. The results show that the composite coatings obtained through HAD/MPO on A3 steel consist of four layers. From the surface to the substrate, the layer is loose Al2O3 ceramic, compact Al2O3 ceramic, At and FeAl intermetallic compound layer in turn. The adhesions among all the layers are strengthened because the ceramic layer formed at the At surface originally, FeAl intermetallic compound layer and substrate are combined in metallurgical form through mutual diffusion during HAD process. Initial experiment results disclose that the anti-corrosion performance and wear resistance of composite coating are obviously improved through HAD/MPO treatment.

Karta öfver Finland (Sektionen A3)

1 kartta :, vär. ;, 50,6 x 43 cm, lehti 58 x 50,3 cm

Optimización y validación de un método analítico por CLAR fase reversa para el análisis de peroxisomicinas A2, A3 e isoperoxisomicinas A1 y A2

Tesis (Maestría en Ciencias con Especialidad en Química Analítica Biomédica) UANL

Proyectos de transición entre ciclos: de 0-3 a3-6.

En este artículo se habla del plan de acogida y adaptación de los alumnos y familias en la escuela.

Oxygen/Glucose deprivation induces a reduction in synaptic AMPA receptors on hippocampal CA3 neurons mediated by mGluR1 and adenosine A3 receptors

Hippocampal CA1 pyramidal neurons are highly sensitive to ischemic damage, whereas neighboring CA3 pyramidal neurons are less susceptible. It is proposed that switching of AMPA receptor (AMPAR) subunits on CA1 neurons during an in vitro model of ischemia, oxygen/glucose deprivation (OGD), leads to an enhanced permeability of AMPARs to Ca2+, resulting in delayed cell death. However, it is unclear whether the same mechanisms exist in CA3 neurons and whether this underlies the differential sensitivity to ischemia. Here, we investigated the consequences of OGD for AMPAR function in CA3 neurons using electrophysiological recordings in rat hippocampal slices. Following a 15 min OGD protocol, a substantial depression of AMPAR-mediated synaptic transmission was observed at CA3 associational/commissural and mossy fiber synapses but not CA1 Schaffer collateral synapses. The depression of synaptic transmission following OGD was prevented by metabotropic glutamate receptor 1 (mGluR1) or A3 receptor antagonists, indicating a role for both glutamate and adenosine release. Inhibition of PLC, PKC, or chelation of intracellular Ca2+ also prevented the depression of synaptic transmission. Inclusion of peptides to interrupt the interaction between GluA2 and PICK1 or dynamin and amphiphysin prevented the depression of transmission, suggesting a dynamin and PICK1-dependent internalization of AMPARs after OGD. We also show that a reduction in surface and total AMPAR protein levels after OGD was prevented by mGluR1 or A3 receptor antagonists, indicating that AMPARs are degraded following internalization. Thus, we describe a novel mechanism for the removal of AMPARs in CA3 pyramidal neurons following OGD that has the potential to reduce excitotoxicity and promote neuroprotection