Glucose, galactose, mannose, arabinose, xylose, rhamnose, fucose, ribose (trace), uronic acid, and five unidentified sugars were chromatographically separated from hydrolysates of polysaccharides extracted from soil which had been incubated with glucose-l-C

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Cathepsin D is an aspartyl lysosomal protease that catalyzes protein cleavage. It is involved in the process of tumor invasion and metastasis. The cathepsin D enzyme has been considered as a potential target for cancer therapy. The objective of this research is to prepare functional recombinant cathepsin D enzyme which will be used in the development of new cathepsin D inhibitors. Human procathepsin D cDNA, purchased from OpenBiosystems, was amplified by PCR and sub‐cloned into XhoI site of pET15b. The procathepsin D‐pET15b construct was then transformed into JM109. The recombinant plasmid was isolated from the JM109 and transformed into BL21(DE3)pLysS cells for expression. Expression of recombinant procathepsin D protein in the transformed BL21(DE3)pLysS cells was induced with IPTG. The level of expression was analyzed by SDS‐PAGE. High level expression (greater than 50% of total cellular proteins) of the His‐tagged procathepsin D fusion protein was achieved when cells were grown in terrific broth. The ability to produce procathepsin D enzyme will permit a drug discovery program for development of newer effective inhibitors of cathepsin D in the near future.Supported by National Cancer Institute at NIH Grant No. 3R15CA086933‐04 and 3R15CA086933‐04A2S1)

Cathepsin B is a lysosomal cysteine proteinase that is implicated in the processes of tumor invasion, metastasis, and Alzheimer's disease. Development of specific inhibitors of cathepsin B could lead to the discovery of therapeutic agents for treatment of many types of carcinomas, as well as Alzheimer's disease. The objective of this research is to produce functional recombinant cathepsin B enzyme which will be used in screening of new cathepsin B inhibitors. Human procathepsin B cDNA has been successfully amplified by PCR and sub‐cloned into pET15b expression vector. Overexpression of the procathepsin B protein has been accomplished by IPTG induction. The ability to produce large quantities of procathepsin B enzyme will permit a drug discovery program for development of newer effective inhibitors of cathepsin B.Supported by National Cancer Institute at NIH (Grant No. 3R15CA086933‐04 and 3R15CA086933‐04A2S1)