麦冬多糖对正常和实验性糖尿病小鼠血糖的影响

目的：研究麦冬多糖对正常和实验性糖尿病小鼠血糖的影响。方法：昆明种小鼠４０只，分成４组，分别用麦冬多糖（１００和３００ｍｇ／ｋｇ）、优降糖（２．５ｍｇ／ｋｇ）和等体积生理盐水（２ｍｌ／只）灌胃，测定各组正常小鼠的血糖水平及以葡萄糖（２ｇ／ｋｇ）、四氧嘧啶（７０ｍｇ／ｋｇ）、肾上腺素（０．０２ｍｇ／ｋｇ）所致小鼠高血糖模型的血糖水平。结果：剂量为１００和３００ｍｇ／ｋｇ的麦冬多糖灌胃对葡萄糖、四嘧啶     

An electron microscopic study of Aujeszky's disease

Summary Sixteen calves were killed at intervals during the course of the disease from 48 h onwards after subcutaneous infection with Aujeszky's disease virus. Ultrastructural changes were evident in the spinal ganglia from 84 h post-inoculation and the intercostal nerves from 96 h post-inoculation. The cytopathic changes in the spinal ganglia consisted of neuronal degeneration, neuronophagia, Schwann cell degeneration and cellular infiltration. The neuronophagic nodule was invariably contained within an intact sheath of satellite cells. Changes in the intercostal nerves were less dramatic but cellular infiltration was frequently seen and occasional Schwann cells were degenerate. In the terminal stages of the disease demyelination was rarely observed. In the ganglion virus was invariably seen in degenerating neurons and occasionally in Schwann cells and monocytes. Satellite cells were rarely infected even when ensheathing an infected neuron. Extra-cellular virus was not observed in ganglia or nerves. Schwann cells and monocytes in the nerves were occasionally infected. Virus particles were seen in the axoplasm both in the ganglion and in the entire length of the nerve. The particles in the axoplasm varied in morphology; thus unenveloped and enveloped particles, and particles in the process of acquiring an envelope were recognised. It was concluded that the neural pathway of Aujeszky's disease virus is probablyvia the axoplasm.     

Ethanol oxidizing enzyme activites in liver disease.

1 The activites of hepatic alcohol dehydrogenase, catalase and the reduced nicotinamide adenine dinucleotide phosphate (NADPH) dependent ethanol oxidizing system were determined in liver biopsies from nine patients with liver disease and seven control subjects with non evidence of liver disease. 2 Alcohol dehydrogenase and catalase activites were significantly lower in the patients with liver disease. 3 The activity of the NADPH dependent ethanol oxidizing system was significantly greater in the patients with liver disease, when its activity was expressed in terms of mg protein or g wet weight liver. 4 It is suggested that the greater activity of the NADPH dependent system may compensate for the low alcohol dehydrogenase activites found in patients with liver disease and maintain normal rates of ethanol metabolism.     

Percutaneous needle localization of clustered mammary microcalcifications prior to biopsy

Mammography occasionally reveals the presence of suspicious appearing clustered microcalcifications without an associated mass. Clinical localization of these microcalcifications within the breast is difficult, even using the 2 dimensional effect of a mammogram. Percutaneous needle localization of these microcalcifications is recommended for its accuracy, patient acceptance, and reduction in size of the biopsy specimen. No complications of this procedure have been encountered.     

Cysteine 2.59(89) in the second transmembrane domain of human CB2 receptor is accessible within the ligand binding crevice: evidence for possible CB2 deviation from a rhodopsin template

In this study, the sensitivity of the CB2 receptor to methanethiosulfonate (MTS) derivatives was tested, and a native cysteine residue conferring the sensitivity was identified. By incubating human embryonic kidney 293 cells stably transfected with CB2 receptors and MTS derivatives such as MTS ethylammonium (MTSEA), [(3)H]HU-243 binding was inhibited. Pretreatment of the CB2 receptor with cannabinoid ligands prevented this inhibition, suggesting that MTSEA modification occurred within the binding crevice. To identify the cysteine(s) responsible for the MTSEA sensitivity, 10 CB2 mutants were prepared in which the eight cysteines in transmembrane domains or extracellular loop 2 were mutated to serine or alanine, one at a time or in combination. Five mutants exhibited specific [(3)H]HU-243 binding, with K(d) and B(max) values similar to those of wild-type CB2. However, five other mutants had no detectable ligand binding and were not detected on cell membranes by Western blot analysis. Among the five mutants with normal binding, only the sensitivity to MTSEA of the C2.59(89)S mutant was reduced significantly. These data demonstrate that C2.59(89) is the residue that mainly confers the inhibitory effect of MTSEA on ligand binding. Furthermore, the magnitude of the second-order rate constant (1.14 +/- 0.28 M(-1)s(-1)) for the MTSEA reaction with wild-type CB2 suggests that C2.59(89) resides at the margin of the CB2 binding site crevice. The accessibility of C2.59(89) to MTSEA provides experimental evidence for a possible conformational difference between TMH2 of CB2 versus Rho. Modeling studies undertaken to explore the origin of such differences suggest it is possibly caused by the conformational influence of S2.54(84).