Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.9 (glucose-6-phosphatase)
 3,081 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A surgical model of EstoRex ultrasound destroyer operating at a frequency of 60 KHz, power of 6 W, and vibration amplitude at the tip of the tool of 15 microns was used to make incisions on rat liver. 5 to 7 s or 24 hr after surgery the specimens of the wound wall were fixed and further processed for electron microscopy and histochemical visualization of glucose-6-phosphatase at the ultrastructural level. In a separate series 2 mm-thick strips of the tissue were excised from the liver, processed by the destroyer for 45 s, and then exposed to a digestion treatment with mixture of trypsin and chymotrypsin for 24 hr at 37 degrees C or in solution of cathepsin L for 60 hr at 25 degrees C. The results showed that ultrasound caused not only thermal but also nonthermal ultrastructural and histochemical alterations, due probably to cavitation and viscous stresses. The ultrasound wound did not contain any proteolytically resistant material. Since ultrasound-processed tissue turned out to be highly susceptible to proteolytic digestion we suggest that the ultrasound destroyer, unlike Nd:YAG laser surgical instrument, would be a promising surgical tool with respect to wound cleaning and healing.
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PMID:[Morphofunctional characteristics of wound inflicted by an ultrasonic destroyer]. 133 73

Two SH-dependent proteinases (I and II) active in neutral media were isolated from bovine spleen and purified to apparent homogeneity. The histone-hydrolyzing activity of proteinase I was increased 3500-fold as compared to that of the original extract. Proteinase I hydrolyzed a variety of proteins (histones, azocasein, hemoglobin, collagen) but did not hydrolyze low molecular weight synthetic substrates, such as BAPA, BANA, BAEE, ATEE, Leu-beta-NA, Arg-beta-Na and Ala-beta-NA. The molecular weight of the enzyme as determined by SDS electrophoresis was found to be about 23,000. Isoelectrofocusing of the enzyme resulted in one major component with pI of 6.05 and in two minor components with pI of 6.2 and 6.4. Proteinase II hydrolyzed Leu-beta-NA, Arg-beta-NA and Ala-beta-NA but did not hydrolyze beta-naphthylamides of dicarboxylic acids and Gly-Phe-beta-Na. This proteinase split BANA and histone and very slowly split azocasein and collagen. Proteinase II was found to have a molecular weight of 30 000 and a pI of 6.8-6.9. Proteinase I inactivated fructose-1.6-diphosphate aldolase, partly inactivated glucose-6-phosphatase dehydrogenase and caused activation of phosphodiesterase of cyclic nucleotides. Proteinase II had no effect on the activity of the above enzymes. A comparison of proteinase I and II with enzymes described in literature demonstrated that the former was cathepsin L, while the latter was cathepsin H from spleen.
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PMID:[Characteristics of two thiol proteinases from spleen active in neutral media]. 675 12