[The history and influence of Losheng Sanatorium in Taiwan area].

Losheng Sanatorium, as a prophylactic-therapeutic institution for isolation, treatment, rehabilitation and social control of leprosy patients, was established by the Japanese colonial government in Taiwan in 1930. Losheng Sanatorium effectively carried out the compulsory isolation of leprosy patients, under the assistance of the public medical system with the help of police and the Bao-Jia management in the Japanese colonial period in Taiwan. Losheng sanatorium imported DDS, a therapeutic drug for leprosy, popularised an outpatient treatment model of leprosy, and developed mobile medical services after the Second World War. Losheng detected and treated leprosy patients successfully through the support of special skin clinics in public hospitals and missionary hospitals after Multi-drug Therapy was introduced in Taiwan in 1984. The Department of Health, Executive Yuan of the Taiwan area in commenced administration of Losheng Sanatorium in 1999 transformed it into a community-based general hospital. Losheng sanatorium adopted different control strategies in different historical periods based on the requirements of health, epidemic prevention systems and leprology developments to achieve its goals of leprosy control. The Sanatorium provides an example to understand and further study epidemical control and public health practice in the Taiwan area.

Thioredoxin reductase-thioredoxin fusion enzyme from Mycobacterium leprae: comparison with the separately expressed thioredoxin reductase.

Thioredoxin reductase (TrxR) catalyzes the reduction of thioredoxin (Trx) by NADPH. A unique gene organization of TrxR and Trx has been found in Mycobacterium leprae, where TrxR and Trx are encoded by a single gene and, therefore, are expressed as a fusion protein (MlTrxR-Trx). This fusion enzyme is able to catalyze the reduction of thioredoxin or 5,5'-dithiobis(2-nitrobenzoic acid) or 1, 4-naphthoquinone by NADPH, though the activity is much lower than that of Escherichia coli TrxR. It has been proposed that a large conformational change is required in catalysis of E. coli TrxR. Because the reductase portion of the enzyme from M. leprae shows significant primary structure similarity with E. coli TrxR, it is possible that MlTrxR-Trx may require a similar conformational change and that the change in conformation may be affected by the tethered Trx. The reductase has been expressed without Trx attached (MlTrxR). As reported here, comparison of the steady-state and pre-steady-state kinetics of MlTrxR-Trx with those of MlTrxR suggests that the low reductase activity of the fusion enzyme is an inherent property of the reductase, and that any steric limitation caused by the attached thioredoxin in the fusion protein makes only a minor contribution to the low activity. Titration of MlTrxR-Trx and MlTrxR with 3-aminopyridine adenine dinucleotide phosphate (AADP+), an NADP(H) analogue, results in only slight quenching of FAD fluorescence, suggesting an enzyme conformation in which the binding site of AADP+ is not close to the FAD, as in one of the conformations of E. coli TrxR.