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

This report demonstrates that a single set of identical synthetic multifunctional pores can detect the activity of many different enzymes. Enzymes catalyzing either synthesis or degradation of DNA (exonuclease III or polymerase I), RNA (RNase A), polysaccharides (heparinase I, hyaluronidase, and galactosyltransferase), and proteins (papain, ficin, elastase, subtilisin, and pronase) are selected to exemplify this key characteristic of synthetic multifunctional pore sensors. Because anionic, cationic, and neutral substrates can gain access to the interior of complementarily functionalized pores, such pores can be the basis for very user-friendly screening of a broad range of enzymes.
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PMID:Enzyme screening with synthetic multifunctional pores: focus on biopolymers. 1453 Apr 13

The interaction of washed cocci, prepared under specified conditions, and a polynucleotide (AF) results in the formation of streptolysin S provided a fermentable carbohydrate is present. Maximum toxin formation requires, in addition, the presence of magnesium, potassium, and phosphate ions. Streptolysin S production proceeds anaerobically as well as aerobically but under the latter condition, apparently only if the system is sufficiently reducing. Temperature has a marked effect on the rate of appearance of toxin, the critical thermal increment having a value of approximately 36,000. The formation of streptolysin S is inhibited by mercuric ion, arsenite, iodoacetate, dinitrophenol, azide, and other enzyme poisons. The development of streptolysin S in resting cell systems depends neither upon autolysis nor upon physical extraction of preformed toxin but upon toxin synthesis. From the supernatant fluid of the resting cell system, a product containing 20,000 to 30,000 units of streptolysin S per mg. dry weight can be isolated. Information concerning the pH stability of the product is presented. The product is free of streptokinase, hyaluronidase, and proteinase, but possesses appreciable desoxyribonuclease activity. Chemical analyses and other findings indicate that polynucleotide and carbohydrate are present in major amount, and that a small but undetermined quantity of protein is present. Inactivation of streptolysin S by chymotrypsin, ficin, papain, or cathepsin, and not by a variety of other enzymes, indicates that protein is essential for activity, but the precise chemical composition of the toxin remains to be established.
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PMID:Formation of a bacterial toxin (streptolysin S) by resting cells. 1814 84