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)

The ascites form of a chemically induced guinea pig hepatoma, line-10, was resistant to killing in vitro by xenogeneic antibody and guinea pig complement. Pretreatment of line-10 cells with certain proteolytic enzymes rendered tham susceptible to the killing action of antibody and guinea pig complement. The effects of enzyme pretreatment were dependent on enzyme concentration, temperature, and could be blocked by addition of competitive or non-competitive inhibitors. The effect of the enzyme treatment could reversed by incubating the treated cells at 37 degrees C (but not at 0 degrees C), in the absence of the enzyme. Effective enzymes included ficin, bromelain, pronase, elastase, papain, trypsin, collagenase, lipases type I and type VI, and the neuraminidase preparation isolated from Clostridium perfringens. The activity of the lipase preparations and the neuraminidase preparation isolated from Clostridium perfringens appeared to be caused by proteolytic enzyme contamination. Enzyme preparations that proved ineffecitve in rendering the line-10 cells sensitive to killing by antibody and guinea pig complement included DNase, RNase, beta-glucuronidase type 6A or type B10, hyaluronidase type V or type VI, and pectinesterase.
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PMID:Lysis of tumor cells by antibody and complement. VI. Enhanced killing of enzyme-pretreated tumor cells. 17 70

Five strains of obligately anaerobic, pectin-fermenting spirochetes were isolated from the subgingival plaque of humans. The strains produced two extracellular enzymatic activities that functioned in pectin degradation. One of these enzymatic activities was pectin methylesterase (EC 3.1.1.11), and the other was pectate lyase (EC 4.2.2.2) of the endo type. The data indicate that the cumulative action of these two enzymatic activities brought about depolymerization of pectin in spirochete cultures. Pectin- or polygalacturonate-degrading hydrolases were not detected. A cell-associated lyase activity that catalyzed polygalacturonate breakdown was present in one of the spirochete strains. In addition to pectin, the isolates utilized polygalacturonic, glucuronic, or galacturonic acid as fermentable substrate but did not neutral sugars, amino acids, or other substrates tested. Although the oral spirochetes did not ferment hyaluronic acid, one of the strains grew in coculture with a hyaluronidase-producing Peptostreptococcus strain in a medium containing hyaluronic acid as fermentable substrate. Two of the isolates were identified as Treponema pectinovorum strains on the basis of their substrate utilization pattern, end products of fermentation, other phenotypic characteristics, and the guanine-plus-cytosine content of their DNA. Even though the pectinolytic isolates were specialized with respect to the fermentable substrates they utilized, they appeared to compete successfully with other microorganisms in their habitat.
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PMID:Pectinolytic enzymes of oral spirochetes from humans. 638 18