Role of Dislocation Scattering on the Electron Mobility of n-Type Long Wave Length Infrared HgCdTe on Silicon

It has been reported that the basic electrical properties of n-type long wave length infrared (LWIR) HgCdTe grown on silicon, including the majority carrier mobility (μ _e) and minority carrier lifetime (τ), are qualitatively comparable to those reported for LWIR HgCdTe grown on bulk CdZnTe by molecular beam epitaxy (MBE). Detailed measurements of the majority carrier mobility have revealed important differences between the values measured for HgCdTe grown on bulk CdZnTe and those measured for HgCdTe grown on buffered silicon substrates. The mobility of LWIR HgCdTe grown on buffered silicon by MBE is reported over a large temperature range and is analyzed in terms of standard electron scattering mechanisms. The role of dislocation scattering is addressed for high dislocation density HgCdTe grown on lattice-mismatched silicon. Differences between the low temperature mobility data of HgCdTe grown on bulk CdZnTe and HgCdTe grown on silicon are partially explained in terms of the dislocation scattering contribution to the total mobility.     

便携式TDICCD遥感相机成像检测系统设计

针对原有TDICCD相机成像检测系统的体积庞大、移动困难、功耗大、不利于外场实验的问题,设计了一套便携式航天遥感相机成像检测系统。首先给出了TDICCD相机的结构以及图像输出时序,然后具体介绍了便携式成像检测系统的硬件设计以及软件设计,最后对某TDICCD相机进行了检测试验,处理10 min遥感图像的时间为10 s,系统现已稳定工作时间为3 000 h,实现了对图像数据和辅助数据的全自动判读,对相机的工作异常进行自动报错处理,判读准确、快速,节省了人力并降低了误判率。本文所研制的便携式成像检测系统工作稳定,适合外场实验,可靠性高。     

Intracellular retention of mutant gonadotropin receptors results in loss of hormone binding activity of the follitropin receptor but not of the lutropin/choriogonadotropin receptor

It has recently been reported that Asp 397 of the rat lutropin/ choriogonadotropin receptor (rLHR) may be involved in transducing the signal from hormone binding to the stimulation of cAMP production. We examined the analogous region in the rat follitropin receptor (rFSHR) by substituting the Asp at position 404 (D404) of the rFSHR with either Glu (D404E), Ala (D404A), or Lys (D404K). Both in intact 293 cells and in detergent-solubilized extracts of 293 cells transiently transfected with the rFSHR constructs, only the wild type rFSHR exhibited detectable binding activity. Although the D404-substituted rFSHR mutants were visible on Western blots, in contrast to the wild type rFSHR which is present on Western blots as both mature and immature forms, only a single band comigrating with immature receptor was observed for the mutants. Furthermore, these mutants were sensitive to endoglycosidase H (Endo H), thus indicating that the mutant receptor proteins were retained intracellularly in the endoplasmic reticulum. To test whether the lack of binding of the D404-substituted rFSHR mutants was due to a perturbation of a binding site or to the intracellular retention of the mutants, a truncated rFSHR(t637) mutant, containing a cytoplasmic truncation that should not directly affect FSH binding, was examined. As with the D404-substitution mutants, rFSHR(t637) was stably expressed but sensitive to Endo H. Significantly, detergent-soluble extracts of cells expressing rFSHR(t637) were unable to bind FSH. From these results, we conclude that substitution of D404 of the rFSHR prevents hormone binding as a result of the intracellular retention of the mutants in the endoplasmic reticulum presumably in an incompletely folded state, as opposed to disruption of a hormone-binding site at D404. Comparable rLHR substitution (D397K) and truncation (t616) mutants were constructed and used to transfect 293 cells. For both rLHR(D397K) and rLHR(t616), human CG (hCG) binding to intact cells was not detectable, but high affinity hCG binding was observed in detergent-soluble extracts of the cells. Therefore, the rLHR differs from the rFSHR in that mutants of the rLHR that are retained in the endoplasmic reticulum have already been folded correctly and can bind hCG with high affinity as long as a hormone-binding site has not been perturbed by the mutation. In contrast, mutants of the rFSHR that are retained in the endoplasmic reticulum have not yet folded into a conformation that can bind hormone. This suggests a difference in the temporal pattern of folding between the two structurally related gonadotropin receptors. Our studies also demonstrate how mutagenesis studies of the rFSHR must be interpreted with caution, as FSHR mutants that are expressed but are retained intracellularly will most likely not be able to bind FSH even when a hormone-binding site has not been altered.     

Mitochondrial genome damage associated with cigarette smoking

We have investigated the level of mitochondrial DNA (mtDNA) damage and deletions in bronchoalveolar lavage tissues from smokers and nonsmokers using quantitative, extra-long PCR and a "common" mtDNA deletion assay. Smokers had 5.6 times the level of mtDNA damage, 2.6 times the damage at a nuclear locus (beta-globin gene cluster), and almost 7 times the level of a 4.9-kb mtDNA deletion compared to nonsmokers, although the latter increase was not significant. Although both genomes (mitochondrial and nuclear) showed significantly increased levels of DNA damage in smokers (mtDNA P = 0.00072; beta-globin P = 0.0056), the relative differences were greatest in the mtDNA. Damage to the mtDNA may inhibit oxidative phosphorylation and, therefore, potentially cause or contribute to chronic lung disease and cancer. Consequently, the mtDNA may be a sensitive biomarker for environmentally induced genetic damage and mutation.