Left ventricle segmentation in dynamic cardiac CT using random walks method.

PURPOSE: Segmentation of the left ventricle (LV) in cardiac CT (CCT) images is difficult due to the intensity heterogeneity arising from accumulation of contrast agent in papillary muscle and trabeculae carneae. In this study, we demonstrated the random walks method for LV segmentation in CCT through cardiac phases. METHODS: 63 CCT data sets from 7 patients with 9 cardiac phases were included in this study. All cardiac CT examinations were performed with GE 64-detector CT scanner with ECG gating. In each patient, 60-80 ml iohexol was injected at a flow rate of 5 ml/sec followed by 60 ml normal saline solution. Random walks (RW) based on probability of labels was used for LV segmentation. The LV delineations generated by the experienced physician (MD), conventional image-based method (IB), and RW were compared. RESULTS: In general the contours segment the LV closely by RW and MD, but the discrepancies in papillary muscle and trabeculae carneae were observed while using the IB method. CONCLUSION: We showed the RW method potentially improved LV segmentation as compared to the volume by conventional IB method. In this study, we demonstrated the clinical feasibility of LV volume segmentation using random walks algorithm.

Characterization of a thermophilic L-rhamnose isomerase from Thermoanaerobacterium saccharolyticum NTOU1.

L-rhamnose isomerase (EC 5.3.1.14, L-RhI) catalyzes the reversible aldose-ketose isomerization between L-rhamnose and L-rhamnulose. In this study, the L-Rhi gene encoding L-Rhi was PCR-cloned from Thermoanaerobacterium saccharolyticum NTOU1 and then expressed in Escherichia coli. A high yield of the active L-RhI, 9780 U/g of wet cells, was obtained in the presence of 0.2 mM IPTG induction. L-RhI was purified sequentially using heat treatment, nucleic acid precipitation, and anion-exchange chromatography. The purified L-RhI showed an apparent optimal pH of 7 and an optimal temperature at 75 °C. The enzyme was stable at pH values ranging from 5 to 9, and the activity was fully retained after a 2 h incubation at 40-70 °C. L-RhI from T. saccharolyticum NTOU1 is the most thermostable L-RhI to date, and it has a high specific activity (163 U/mg) and an acceptable purity after heat treatment, suggesting that this enzyme has the potential to be used in rare sugar production.