Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

Glycosaminoglycan-protein complexes were extracted from bovine duodenal mucosa with distilled water, resulting in solubilization of a fraction of the total proteoglycan of the tissue. The extracted material was purified by anion exchange chromatography on DEAE-Sephadex A-25, and then characterized by chemical analysis and by fractionation on Dowex 1. By using these procedures, two major fractions were identified, which were eluted from Dowex with 1.0-1.25 M NaC1 and with 1.5-1.75 M NaC1 respectively. Analyses showed that both fractions were mainly composed of glucosamine-containing, hyaluronidase-resistant polysaccharides, which were identified by their N-sulphate: D-glucosamine and total sulphate: D-glucosamine ratios as heparan-sulphate in the less acidic fraction, and as heparin in the more acidic fraction. Dermatan sulphate molecules were also present in both preparations, with an approximate ratio 1:3 to the glucosamine-containing polysaccharides. Solubility behaviour of the complexes formed by the isolated polyanionic molecules with cetylpyridinium chloride was strongly modified by papain digestion of the duodenal material. This reduction of molecular size of papain treatment suggests that the molecules extracted with water from duodenal mucosa are complex proteoglycans, perhaps in the native state.
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PMID:Water soluble proteoglycans from bovine duodenal mucosa. 88 4

The present study was undertaken in order to characterize further the glycosaminoglycans of normal human plasma. Coagulation factor IX concentrate prepared from undiluted plasma by DEAE-Sephadex chromatography was used as the starting material. The concentrate was subjected to proteolytic treatment with papain and pronase, deproteinised with trichloroacetic acid, dialysed and passed through an AG 1 X 2 anion-exchange column. Glycosaminoglycans were eluted stepwise from the column with NaC1. The sole glycosaminoglycan obtained was an undersulphated chondroitin-4-sulphate which was identified by chemical analyses, digestibility with testicular hyaluronidase, electrophoretic behaviour and infrared spectrum. Gel-exclusion chromatography indicated a molecular weight of 17 000 for the compound. The undersulphated chondroitin-4-sulphate was calculated to represent at least 80% of the macromolecular glycosaminoglycans present in normal human plasma and to occur in a concentration of approx. 3 mg hexuronate per 1 of plasma.
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PMID:Isolation and characterization of undersulphated chondroitin-4-sulphate from normal human plasma. 118 96

The author presents a so far unknown pathological process interrupting permanently the regeneration of the superficially damaged cornea, and its consequences and therapy of the condition as well. The process occurs only in 5.6% of the injured individuals. The occurrence is in no correlation with the quality or extent of the damage. Also it is independent of the form and duration of therapy. The essence of the pathological changes is the slowing of corneal epithelisation within 2-4 days, followed by a complete cessation. After that a thin membrane-like layer develops simultaneously and evenly within 12 days on the area without epithelium, the surface of which is dull, transparent and whitish in colour. Within weeks or months an individually varying thickening of the membrane occurs, but the area does not grow. The surface becomes whitish-grey and is without any epithelium and with no adherence to tear. The deposits are closely and inseparably adherent to their base, their substance is rigid, being brittle only at the margins. The lesion is staining greenish-yellow with Na-fluorescein, and lively blue with toluidine blue. It is staining in small reddish-brown with rose bengal. In vivo the deposits are not measurably influenced by hyaluronidase, trypsin, alpha-chymotrypsin and papain. The microbes play no role in the process. Histological and electron-microscopical examinations suggest the corneal deposit are the product of the necrobiotic process occurring on the corneal surface during regeneration. The specific treatment consists of local application of corticoid-heparin. On the basis of the results of the examinations and literary data the author suggests that the corneal deposition and the similarly rare KCV (keratoconjunctivitis vernalis) plaque formation is the same specific process, i.e. the peculiar manifestation of the atopic state of the organism occurring independently of age.
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PMID:Ceasing of epithelisation and deposit formation of unknown origin on the cornea. 172 62

Enzymes are often used for preparation of excitable tissues. The effects of papain, trypsin, pronase, collagenase and hyaluronidase on the photoreceptor function were studied by recording of scotopic PIII responses. Each enzyme treatment diminished the amplitudes of the PIII responses with a characteristic time course. The effects of papain, collagenase and hyaluronidase were at least partly reversible, while trypsin and pronase irreversibly reduced the amplitudes of the PIII responses.
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PMID:Enzyme treatment of photoreceptors: effects on the scotopic PIII component of the frog electroretinogram. 196 26

To maintain the hatchability of miracidia, pure worm eggs of S. mansoni were collected in great quantities from liver and spleen of experimentally infected mice. For this purpose, the tissue was digested with papain, hyaluronidase and trypsin. Worm eggs in the residue were separated from remaining host cells, tissue materials and dead eggs by using the sieving chamber (sieves 200 microns x 200 microns and 28 microns x 28 microns) and by density gradient centrifugation.
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PMID:[Preparative representation of the living eggs of Schistosoma mansoni]. 212 71

Physiological stimuli induce rapid and unexplained increases in the number of red blood cells within capillaries of skeletal muscle. We hypothesized that such alterations in intracapillary red cell numbers might be due to an undefined interaction between one or more components of blood and the luminal surface of the capillary. This proposition was tested by in situ microperfusion of capillaries with enzymes directed against macromolecules likely to be expressed on the surface of endothelial cells. The instantaneous fractional volume of red blood cells within a capillary (tube hematocrit) was used as an index of a capillary's response to enzyme microperfusion. Five to 8 min of perfusion with enzyme vehicle (0.25% albumin-Ringer solution) produced no significant alteration in capillary tube hematocrit. Perfusion with solutions containing heparinase raised the tube hematocrit at least twofold (P less than 0.05) without a significant change in red cell velocity. Heat-denatured heparinase and other enzymes such as neuraminidase, hyaluronidase, papain, pronase E, and clostripain had no detectable effect on the tube hematocrit (P greater than 0.05). After enzyme treatment, application of adenosine (10(-4) M) or oxygen caused brisk vasomotor responses in arterioles feeding perfused capillary units, but the usual changes in the tube hematocrit were not observed. Thus heparinase treatment results in a sustained elevation in the capillary tube hematocrit and a dissociation of the typical relationship between vasomotor changes and red cell distribution in capillaries. These findings suggest that physiological stimuli which alter the number of red blood cells within capillaries may operate by modifying interactions between plasma and one or more components on the luminal surface of capillaries.
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PMID:Heparinase treatment suggests a role for the endothelial cell glycocalyx in regulation of capillary hematocrit. 231 79

The chemical nature of anionic sites located on both fronts of the endothelial cells (ECs) and in the basement membrane (BM) of mouse brain capillaries was studied using tissue sections embedded in Lowicryl K4M and cationic colloidal gold. Before labelling with cationic probe, the sections were digested with the following enzymes: trypsin, papain, pronase E, proteinase K, collagenase, chondroitinase ABC, hyaluronidase, heparinase, heparitinase, neuraminidase and endoglycosidase H. The results indicate that the negatively charged surface layer on the luminal front differs in chemical nature from that on the abluminal front of the EC. Anionic sites located on the luminal surface of the plasmalemma of the ECs are mainly contributed by sialic acid residues of acidic glycoproteins. On the contrary, the anionic domains on the abluminal front of the EC represent mixed proteoglycan and acid glycopeptides containing hydrophobic amino acids, sialic acid residues, and are rich in heparan sulphate-bearing glycosaminoglycans. The anionic sites of the BM are contributed in a substantial degree by chondroitin and heparan sulphate-rich glycosaminoglycans. The effect of endoglycosidase H suggests that glycopeptides containing oligomannosyl residues linked to N-acetylglucosamine contribute in small degree in maintenance of the negative charge in the BM, but not on the surfaces of the EC. These results show that brain endothelium bears surface anionic domains differing chemically from those described for some fenestrated and continuous endothelia. The distribution of anionic sites indicates that the discrimination against various negatively charged molecules takes place on both fronts of the ECs as well as in the BM of brain micro-blood vessels. The exact role of these domains in the function of the blood-brain barrier remains to be established.
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PMID:Ultracytochemical characterization of anionic sites in the wall of brain capillaries. 274 7

The synthesis of extracellular [35S]-SO4- and [3H]-glucosamine-labelled glycosaminoglycan (GAG) was studied in confluent human gingival fibroblast cultures in vitro. The differential synthesis of the total chondroitin sulphate/dermatan sulphate (CS/DS) and heparan-sulphate (HS) fraction was measured following chondroitinase-ABC digestion, nitrous-acid treatment and column chromatography on Sephadex G50. Control cultures synthesized a CS/DS fraction that represented 78 per cent of the total [35S]-SO4-GAG; the residual 22 per cent was heparan sulphate. Similar cultures were labelled with [3H]-glucosamine and the proportions of a high molecular-weight hyaluronic acid (HA) and proteoglycan fractions measured by gel-filtration HPLC after papain and hyaluronidase digestions. The HA fraction represented 66 per cent of the total isotope incorporated in control cultures. GAG chains released on treatment with papain (24 per cent of the total label incorporated) were of apparent molecular weight 17-20 kDa. All cultures exposed to Bacteroides gingivalis W50 outer membrane at concentrations between 2 and 50 micrograms ml-1 displayed a decrease in the CS/DS fraction and a reciprocal increase in the HS. However, the proportion of HA synthesized was slightly enhanced with a reciprocal decrease in the proteoglycan (papain-digestible) fraction. There was no alteration in the molecular weight of the papain-digestion products or the size distribution of the hyaluronic-acid fraction.
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PMID:The effect of the outer membrane fraction of Bacteroides gingivalis W50 on glycosaminoglycan metabolism by human gingival fibroblasts in culture. 325 24

Although the core protein of a heparan sulfate proteoglycan has been detected in brain microvessel basement membranes by immunoperoxidase staining, cytochemical evidence of a glycosaminoglycan component, in the form of discrete staining with ruthenium red, is not found. To resolve this discrepancy, we examined the glycosaminoglycan content of this basement membrane directly. Microvessels were isolated from pig cerebral cortex, and basement membranes freed from cellular elements. Following digestion with papain and Pronase, the glycosaminoglycans were precipitated with cetyl pyridinium chloride and ethanol. The resulting extract contained uronic acid, and after electrophoresis on Super Sepraphore revealed 2 bands: One co-migrated with heparan sulfate standard, the other with chondroitin sulfate A and C. The first was completely eliminated by nitrous acid and heparitinase, but not by hyaluronidase or chondroitinase ABC and was therefore confirmed as heparan sulfate; the other band was eliminated by chondroitinase ABC but not by the other three treatments. The findings suggest that basement membrane of brain microvessels, like other vascular basement membranes, contains heparan sulfate and chondroitin sulfate A and/or C. The failure of staining with ruthenium red is probably a result of unique structural features of this basement membrane, rather than an absence of glycosaminoglycan.
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PMID:Isolation of glycosaminoglycans from basement membranes of brain microvessels. 334 40

A method for quantifying hyaluronic acid in biological tissues and fluids is described. The assay uses ion-pair HPLC to resolve and quantify the oligosaccharide end products of Streptomyces hyaluronidase digestion. Tissue samples were solubilized by papain, and the nondiffusate after dialysis was exhaustively digested with Streptomyces hyaluronidase. The resulting tetrasaccharide and hexasaccharide cleavage products were resolved by reverse-phase high-performance liquid chromatography in the presence of the ion-pairing agent, tetrabutylammonium phosphate. The saccharides were detected and quantified by their absorbance at 232 nm due to the alpha, beta-unsaturated carboxyl group generated by the eliminase reaction. In control experiments 93 +/- 3% of a hyaluronic acid standard so treated was reproducibly recovered as its tetra- and hexasaccharide cleavage products. As little as 0.5 microgram of the oligosaccharides could be quantified with no interference from a vast excess of chondroitin sulfate or other tissue components. The assay was applied to various types of human, bovine, and rabbit cartilage and to samples of other tissues including nucleus pulposus, annulus fibrosus, skin, aorta, cervix, cockscomb, synovial fluid, and vitreous humor. Results on human articular cartilage showed a linear increase in the content of hyaluronate from 0.1 to 0.5% of tissue dry weight between birth and 80 years of age.
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PMID:Quantitation of hyaluronic acid in tissues by ion-pair reverse-phase high-performance liquid chromatography of oligosaccharide cleavage products. 340 15


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