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

Hyaluronate lyase (hyaluronidase) has been purified and characterized from a group A type 4 Streptococcus. Production of the enzyme was favored by growth in trypsinized veal infusion in the presence of hyaluronate oligosaccharide and tetrasaccharide. Detectable enzymatic activity was diminished in the presence of N-acetylglucosamine and glucuronic acid. Purification of hyaluronate lyase consisted of 40 to 60% ammonium sulfate precipitation, diethylaminoethyl A-50 Sephadex ion-exchange chromatography, gel filtration with G-200 Sephadex, and adsorption to Sepharose 6B. Purified enzyme was antigenically homogeneous and free of proteinase, deoxyribonuclease, streptolysin 0, and streptokinase. Active hyaluronate lyase was recovered from neutral polyacrylamide gels, and it appeared to be a glycoprotein. A single band was detected by sodium dodecyl sulfate-acrylamide electrophoresis, which had a molecular weight of approximately 50,000. A molecular weight of 70,000 was observed by gel filtration. The purified enzyme had a Km of 3.8 x 10(-4) and a pH optimum of 6.0. Reducing agents increased the activity of crude enzyme at least threefold and were necessary to prevent inactivation of the purified enzyme.
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PMID:Purification and properties of streptococcal hyaluronate lyase. 0 65

Urea treatment of a temperate bacteriophage from a type 49 strain of group A streptococcus (Streptococcus pyogenes) followed by ammonium sulfate fractionation, ion exchange, and affinity chromatography of solubilized proteins provided for the recovery (12%) and purification (44-fold) of the phage-associated hyaluronidase. The molecular weight of the homogeneous, purified enzyme was estimated to be 71,000 by polyacrylamide gel electrophoresis (in the presence of sodium dodecyl sulfate) and 75,000 by gel filtration with Sephacryl S-200. The enzyme has a pH optimum of 5.5, a Vmax of 0.1 absorbance unit/min per microgram of protein, and a Km of 4.8 X 10(-2) mg/ml with umbilical cord hyaluronic acid as substrate. Of the cations tested, calcium and magnesium were the only effectors of the enzyme. The enzyme is a glycoprotein (7.25% carbohydrate) containing glucose, galactose, and glucosamine. Analysis of the amino acid composition revealed a predominance of acidic amino acids and a relatively high content of cysteine. The partial specific volume, estimated from the amino acid and sugar analyses, was 0.725 cm3/g.
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PMID:Purification and characterization of a hyaluronidase associated with a temperate bacteriophage of group A, type 49 streptococci. 2 84

Mycobacterium ulcerans produces an exotoxin in culture which, when inoculated into guinea pig skin, causes inflammation, necrosis, edema, and other histopathological changes resembling those in infections of humans. The toxin was resistant to heat and to alkalies and was moderately acid labile. Toxic activity was destroyed by Pronase, phospholipase, lipase, amylase, and glucosidase but not by trypsin, collagenase, cellulase, lysozyme, hyaluronidase, or neuraminidase. Toxic activity was resistant to treatment with 2-mercaptoethanol, urea, guanidine hydrochloride, p-chloromercuribenzoate, ethylenediaminetetraacetate, and sodium deoxycholate but was destroyed by sodium m-periodate and sodium dodecyl sulfate. The toxin was precipitated by a wide range of ammonium sulfate concentrations. Extraction with chlorofrom-methanol or petroleum ether destroyed its activity. Isopycnic density gradient ultracentrifugation in KBr produced a high-density lipoprotein layer with a 24-fold increase in specific activity. The results indicate that this toxin is a high-molecular-weight phospholipoprotein-polysaccharide complex.
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PMID:Further characterization of Mycobacterium ulcerans toxin. 3 Jun 94

The ultrastructural study of liver tissues from 38 patients with type B viral hepatitis consistently showed the presence of hepatitis B core antigen of 21-25 nm size in the liver cell nuclei and to a lesser extent in the cytoplasm. This finding and the demonstration of the tubular form of hepatitis B surface antigen in the proliferative degranulated endoplasmic reticulum constituted the etiologic criterion for the diagnosis of the disease. The double-shelled Dane-like particles were frequently found in association with the tubular form of the surface antigen. The core particles were found in the protoplasmic processes of hepatocytes and this correlated with the immunofluorescent microscopic findings that the antigen may be shed into circulation with the protoplasm. The core antigen was found to resist digestion by various enzymes such as protease, DNase, RNase, phospholipase C, lipase, lysozyme, diastase, neuraminidase and hyaluronidase, all of which did not destroy the immunoreactivity as demonstrated by immunoelectron and immunofluorescent microscopy. Similarly, sodium dodecyl sulfate, Tween 80 and mercaptoethanol also had no effect. The formalin-fixed paraffin-embedded liver tissue sections could be treated with protease to facilitate the immunofluorescent staining for the core antigen in tissue.
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PMID:Structural and immunoreactive characteristics of hepatitis B core antigen. 5 6

Studies were undertaken to define more fully the antigenic properties of human articular cartilage proteoglycans, in anticipation of its potential contribution to alterations arising in diseased states and following cartilage transplantation. Proteoglycans, extracted from normal, adult articular cartilage by dissociative measures, were subjected to purification by cesium density gradient ultracentrifugation, under conditions facilitating both molecular aggregation and dissociation. A polydisperse population of reactive determinants was observed in immunodiffusion and hemagglutination inhibition systems, employing proteoglycan specific antisera on gradient fractions. Highly aggregated proteoglycan species appeared to contain potentially masked antigenic determinants, which were revealed after guanidine dissociation but not hyaluronidase digestion. Polyacrilamide disc gel electrophoresis in sodium dodecyl sulfate, in conjunction with disc elution experiments, confirmed proteoglycan antigenic polydispersity.
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PMID:Polydispersity of human articular cartilage proteoglycan antigens. 6 14

An analysis of 6-phosphofructokinase from brewers' yeast in the presence of sodium dodecylsulfate reveals the occurrence of four components with the following molecular weights: alpha = 140000, beta = 130000, and alpha' = 92000, beta' = 87000. It was found that the alpha- and beta-components can be converted to the alpha' and beta' components by treatment of the native preparation with hyaluronidase. A comparison of the molecular weight obtained by ultracentrifugation and gel filtration with the results obtained by dodecylsulfate electrophoresis after treatment with hyaluronidase reveals that the alpha' and beta' components are the smallest molecular structures obtained upon dissociation of the native enzyme. The mechanism of action of hyaluronidase suggests a desensitization of the alpha and beta components of the enzyme towards dodecylsulfate. Thus, in the absence of hyaluronidase treatment; only an apparent molecular weight for the alpha and beta component is obtained. The analysis indicates that the native enzyme might be composed of four different subunits with an alpha, beta, alpha' and beta' configuration. It is not excluded that the native enzyme consists only of alpha- and beta-chains.
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PMID:Subunit structure of 6-phosphofructokinase from brewers' yeast. 12 16

It has been known for a long time that hearing deficits may coexist in patients with thyroid disease, but without definite morphologic evidence present to correlate gland dysfunction with hearing disturbances. To clarify this relationship between thyroid dysfunction and hearing disturbances, the guinea pig was employed as an experimental model. 70 animals were thyroidectomized, and maintained in a hypothyroid state for varying periods of time. The animals were then sacrificed, and various histochemical studies then performed. These studies included analysis for glycosidase (beta-galactosidase, beta-glucuronidase, n-acetyl-beta-glucosamide), non-specific esterases, sulfatases, sulghydryl groups as well as mucous substances within the cochlea and saccus endolymphaticus of the experimental animals. Results indicated that hyaluronidase-sensitive mucous substances were increased in the scala of the inner ear. As a consequence of increased deposition of acid mucopolysaccharides, the relationship of potassium to sodium in endolymph and perilymph was found markedly altered. Marked swelling of the chambers of the inner ear was noted, and believed to represent hydropic induction by acid mucopolysaccharide-with consequent alteration of electrolyte relationships ("Electrochemical Theory").
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PMID:[Animal experiment histological-histochemical studies on the development of hearing disorders related to hypothyroidism]. 12 84

To investigate the dystrophic influence on the characteristics of actin, a method for the isolation of F-actin filaments from the skeletal muscle of small sizes, i.e., less than 0.5 g, was devised. In this method, minced muscle was treated with collagenase and hyaluronidase, and the isolated filaments were washed with adenosine triphosphate (ATP). Upon examination in the sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the ATP-washed filaments showed a protein component identical in mobility to actin in untreated myofibrils or to that prepared by the conventional method. Electron microscopic appearances of the filaments were similar to those of F-actin filaments described in the literature. The dimensions of the filaments were 0.5--2.5 micrometer in length and 60--70 A in diameter. The ability to activate the Mg-adenosine triphosphatase or myosin was found to be Ca2+ independent. In all aspects of the above characteristics, the filaments from leg muscles of 129/Re dydy dystrophic mice and their litter mates were observed to be identical.
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PMID:Isolation of F-actin filaments. Comparison of F-actin filament preparations from normal and dystrophic mouse muscle. 15 92

Morphologically and functionally intact acinar cells have been obtained from the rat parotid gland through enzymatic dispersion with pure collagenase, hyaluronidase, and trypsin as well as mild mechanical forces. Cell yields of 30-50% of the original tissue weight with over 95% acinar cells were accomplished. The cells in suspension assumed a more or less spherical shape but the intracellular polarity of organelle distribution was maintained. The cells in suspension at 37 degrees C maintained stable monovalent cationic composition but lost potassium and gained sodium rapidly upon exposure to ouabain, 10(-5) M. The intracellular amylase concentration and the patterns of secretion of amylase and of synthesis of cyclic AMP by the cells in response to adrenergic stimulation with epinephrine or isoproterenol were comparable to those of the intact gland in situ. In addition, the cells showed good O2 consumption and maintained it constant for periods up to 8 h. These cells could be used as experimental tools for in vitro studies of receptor physiology and biochemistry, cell membrane function, cellular secretory mechanisms, and other parameters of exocrine gland cell physiology.
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PMID:Dispersed rat parotid acinar cells. I. Morphological and functional characterization. 17 40

Materials released into culture medium by transformed and untransformed baby hamster kidney cells labelled with glucosamine, sulfate, fucose or leucine were characterized. Some of the components could also be labelled by iodination of intact cells, indicating their surface origin. Analysis on gradient polyacrylamide sodium lauryl sulfate gels demonstrated that a group of high apparent molecular weight glucosamine-labelled components were more abundant in materials released from Rous sarcoma virus-transformed baby hamster kidney cells than from baby hamster kidney cells or polyoma virus-transformed baby hamster kidney cells. The relative rates of release of glucosamine-labelled components from transformed and untransformed cells were similar except that the transformed baby hamster kidney cells released some large molecular weight components slightly more rapidly than baby hamster kidney cells. Treatment of labelled medium materials with testicular hyaluronidase removed much glucosamine label from the materials but did not affect the amounts of other labels. After treatment with hyaluronidase, the patterns of labelled conditioned media from both transformed and untransformed baby hamster kidney cells were qualitatively and quantitatively very similar, suggesting that the differences seen in untreated labelled conditioned media were due to the presence of hyaluronidase-sensitive materials associated with medium materials rather than to actual differences in glycoproteins.
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PMID:Materials released into culture medium by normal and oncogenic virus-transformed mammalian cells. 18 66


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