反转构造的反转程度及其与油气聚集的关系

结合典型反转构造地震剖面，分析了断层型和褶皱型两类反转构造的反转程度，上下皆正断层型和向形褶皱型反转构造的反转程度轻微；上逆下正断层型和透镜形褶皱型反转构造的反转程度中等；上下皆逆断层型和背形褶皱型反转构造的反转程度强烈。分析了反转构造的反转程度与油气聚集的关系，处于轻微反转程度的上下皆正断层型反转和向形褶皱型反转，以及处于强烈反转程度的上下皆逆断层型反转和背形褶皱型反转不利于油气聚集；处于中等反转程度的上逆下正断层型反转和透镜形褶皱型反转类型有利于油气聚集成藏。     

利用整合区域特性约束提高孔隙率模拟精度

本文将空间结构变化的要求与动态资料确定的储量共同作为约束,建立了包含两个约束条件的目标函数, 应用模拟退火算法对孔隙率的空间分布进行预测。在实现过程中,通过初始控制参数的给定及目标函数修改提高了运算效率。由于目标函数有效地整合了静、动态信息,从而降低了模拟结果的不确定性．提高了模拟的精度。合成数据及实际数据的模拟试验表明,整合区域特性约束不仅提高了孔隙率模拟精度,而且算法收敛快、稳定性高。     

光学材料的激光微加工研究进展与应用前景

综述了国内外在光学材料激光微加工方面的研究成果和应用状况，并展望了其发展前景。     

Grain Boundary Sliding in Fatigue of Pure Aluminum

The distributions of plastic strain near grain boundaries induced by fatigue loading were investigatedby the fiducial grid method in pure aluminum specimens, and the resulted grain boundary sliding(GBS) was systematically analysed. The results show that the strain field near a grain boundary isnonuniform. GBS is restricted by the junction of grain boundaries and causes discontinuities of bothdisplacement and strain. A peak value of shear strain was created in short-range area across the grainboundary. GBS plays an important role in cyclic softening and secondary hardening. The control fac-tor of GBS is the relative orientation between two grains and the macro orientation of the grainboundary rather than the ∑ value of the boundary.     

注射成形粘结NdFeB磁体:工艺·性能·应用

综合介绍了几种适于注射成形粘结NdFeB磁体的磁粉制备方法及特点；讨论了粘结剂、改性剂及磁场取向对注射成形NdFeB磁体最终磁性能的影响及其应用市场。在此基础上，指出了今后开展研究工作的方向。     

Future directions for the Agency for Health Care Policy and Research

The Agency for Health Care Policy and Research (AHCPR) plays a leading role in health services research. Research efforts to develop practice guidelines, outcomes research, and computer applications have led to improvements in the delivery of care and reduced health care costs. These efforts aid consumers, providers, purchasers, and policy makers in health care decision making. This article cites numerous examples of AHCPR's efforts to increase quality of care and reduce costs.     

1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine as a substrate of cytochrome P450 2D6: allosteric effects of NADPH-cytochrome P450 reductase

1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP), a neurotoxin that produces Parkinsonism symptoms in man, has been examined as a substrate of recombinant human cytochrome P450 2D6. When cumene hydroperoxide is used as an oxygen and electron donor, a single product is formed, identified as 4-phenyl-1,2,3,6-tetrahydropyridine. The K(m) for formation of this product (130 microM) is in agreement with the dissociation constants for MPTP binding to the enzyme determined by optical and nuclear magnetic resonance (NMR) spectroscopy. When the reaction is carried out with nicotinamide adenine dinucleotide phosphate (reduced) (NADPH) and recombinant human NADPH-cytochrome P450 reductase, a second product, identified as 1-methyl-4-(4'-hydroxyphenyl)-1,2,3,6-tetrahydropyridine, is formed in addition to 4-phenyl-1,2,3,6-tetrahydropyridine. The K(m) values for formation of these two products are 19 microM and 120 microM, respectively. Paramagnetic relaxation experiments have been used to measure distances between the protons of bound MPTP and the heme iron, and these have been used to construct models for the position and orientation of MPTP in the active site. For the cytochrome alone, a single mode of binding was observed, with the N-methyl close to the heme iron in a position appropriate for the observed N-demethylation reaction. In the presence of the reductase, the data were not consistent with a single mode of binding but could be explained by the existence of two alternative orientations of MPTP in the active site. One of these, characterized by a dissociation constant of 150 microM, is essentially identical to that observed in the absence of the reductase. In the second, which has a K(d) of 25 microM, the MPTP is oriented so that the aromatic ring is close to the heme iron, in a position appropriate for p-hydroxylation leading to the formation of the product seen only in the presence of the reductase. In the case of codeine, another substrate for cytochrome P450 2D6, the addition of reductase had no effect on the nature of the product formed, the dissociation constant, or the orientation in the binding site. These observations show that NADPH-cytochrome P450 reductase has an allosteric effect on the active site of cytochrome P450 2D6 that affects the binding of some substrates but not others.     

Purification and partial characterization of 76 kDa transglutaminase in the egg envelope (chorion) of rainbow trout, Oncorhynchus mykiss

Transglutaminase (TGase), responsible for crosslinking between proteins, is known to be localized exclusively in the egg envelope (chorion) of rainbow trout, Oncorhynchus mykiss, and probably participates in the post-fertilization chorion hardening. We purified the TGase from unfertilized egg chorions by sequential chromatography using SP-Sepharose, Q-Sepharose, and TSK-gel G3000SWXL columns. The purified enzyme was a monomeric protein having the molecular mass of 76 kDa. It promoted incorporation of monodansyl-cadaverine into chorion protein and catalyzed the polymerization of chorion subunit proteins. The effect of various reagents suggested that the chorion TGase is a Ca2+-dependent SH-enzyme similar to the well-characterized TGases of various animals. The highest activity was observed at pH 6.0. The amines examined in the present study inhibited the TGase activity of the purified enzyme. However, they did not necessarily cause effective inhibition of its activity. These properties of the chorion TGase were essentially consistent with our previous observations on polymerization of chorion proteins, resulting in chorion hardening. We compared the amino acid composition of the purified TGase with those of the previously characterized TGases of fishes, such as chum salmon and red sea bream. The results suggest that the chorion 76 kDa TGase is not homologous with those liver TGases in terms of amino acid composition.     

Fetus-in-fetu with malignant recurrence

Fetus-in-fetu is an unusual condition in which a vertebrate fetus is enclosed within the abdomen of another fetus. These occurrences are usually benign. This report describes an instance of malignant recurrence after resection of a fetus-in-fetu.