Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.36 (hyaluronidase)
4,606 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Polysaccharases release microorganisms from their natural seat, marine sediments for example. The enzymatic activity works both on the microbial adherence polysaccharides and on the support surfaces (cellulose, pectine, etc.). Dosages of glucose confirm polysaccharase activity. An association of bacitracine, thiophenicol and a few enzymes: cellulase, pectinase, amyloglucosidase, alpha amylase, hyaluronidase, release a considerable number of bacteria. The culture on specific mediums confirm the specificity of this release. E. coli polyresistant strain where isolated by amylo-glucosidase, glucuronidase association in a mixture of thiophenicol and bacitracine. Bacillus and other Gram positive bacteria are frequently isolated by this method. The number of colonizer microorganisms on solid media are considerably higher with sediments treated by enzymes, or by enzyme, antibiotic mixtures, than with untreated ones.
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PMID:[Enzymatic release of sedimentary bacteria in the presence of antibiotics]. 682 Mar

Pompe disease (glycogen storage disease type II) is a glycogen storage disease caused by a deficiency of the lysosomal enzyme, acid maltase/acid alpha-1,4 glucosidase (GAA). Deficiency of the enzyme leads primarily to intra-lysosomal glycogen accumulation, primarily in cardiac and skeletal muscles, due to the inability of converting glycogen into glucose. Enzyme replacement therapy (ERT) has been applied to replace the deficient enzyme and to restore the lost function. However, enhancing the enzyme activity to the muscle following ERT is relatively insufficient. In order to enhance GAA activity into the muscle in Pompe disease, efficacy of hyaluronidase (hyase) was examined in the heart, quadriceps, diaphragm, kidney, and brain of mouse model of Pompe disease. Administration of hyase 3000 U/mouse (intravenous) i.v. or i.p. (intraperitoneal) and 10 min later recombinant human GAA (rhGAA) 20 mg/kg i.v. showed more GAA activity in hyase i.p. injected mice compared to those mice injected with hyase via i.v. Injection of low dose of hyase (3000 U/mouse) or high dose of hyase (10,000 U/mouse) i.p. and 20 min or 60 min later 20 mg/kg rhGAA i.v. increased GAA activity into the heart, diaphragm, kidney, and quadriceps compared to hyase untreated mice. These studies suggest that hyase enhances penetration of enzyme into the tissues including muscle during ERT and therefore hyase pretreatment may be important in treating Pompe disease.
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PMID:Hyaluronidase increases the biodistribution of acid alpha-1,4 glucosidase in the muscle of Pompe disease mice: an approach to enhance the efficacy of enzyme replacement therapy. 1702 13