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)

Hyaluronidase from rhesus monkey testes was purified by detergent extraction, ammonium sulphate fractionation, Sephadex G-200 column chromatography and concanavalin A-Sepharose affinity chromatography. The purified hyaluronidase showed one protein band on acrylamide gel electrophoresis. Antibodies to the purified hyaluronidase were raised in rabbits and showed a single precipitin line by Ouchterlony gel diffusion. The enzyme had a molecular weight of 62,000. The Km was 0.5 mg/ml for hydrolysis of hyaluronic acid at 37 degrees C. The optimum pH for the enzyme was 5.0 but activity was present over a broad pH range. The hyaluronidase was inhibited by HgCl2, CuSO4, FeSO4 and p-chloromercuribenzoate all at a concentration of 2 x 10(-4) M. Cysteine protected the enzyme against HgCl2 inhibition.
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PMID:Immunoenzymic studies on testicular hyaluronidase from rhesus monkeys (Macaca mulatta). 680 65

A commercial chromatofocusing system was applied to Cohn's fraction III of human serum to purify hyaluronidase (E.C.3.2.1.3.5). The protein that eluted in the pH range 4.7-5.3 was pooled and precipitated by adding ammonium sulphate to 50% saturation. This sequence of fractionation purified hyaluronidase extensively by immunological criteria. It is shown that hyaluronidase is a population of enzymes displaying microheterogeneity. The commercial chromatofocusing system behaved as theoretically expected. The capacity of the gel is 3 mg per ml gel. Any overload will be trapped or precipitated in the gel. The gel is easy to handle and did not deteriorate on repeated use.
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PMID:Purification of human serum hyaluronidase using chromatofocusing. 709 13

Human liver hyaluronidase was purified to homogeneity by (NH4)2SO4 fractionation, chromatography on hydroxyapatite and DEAE-cellulose, and preparative disc polyacrylamide-gel electrophoresis. The enzyme had a pH optimum of 3.8-4.0, a molecular weight (determined by gel filtration) of 76000, and a Km of 0.05 mg/ml for purified human umbilical-cord hyaluronic acid. It generally resembled hyaluronidases studied in other tissues which are believed to be lysosomal, but shared a number of characteristics with a partially purified bovine testicular hyaluronidase. Neither enzyme exhibited inhibition by high concentrations of substrate, but both were competitively inhibited by dermatan sulphate and keratan sulphate. Both enzymes exhibited increased activity in the presence of albumin, probably owing to an increased susceptibility of substrate to enzyme action. The liver enzyme was inhibited by NaCl, but the testicular enzyme exhibited an increase in activity in the presence of the salt which was similar to the effect observed with albumin. The different response toward Cl- ion appeared to be the most significant difference between the two enzymes.
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PMID:Purification and properties of hyaluronidase from human liver. Differences from and similarities to the testicular enzyme. 712 84

The iodoplatinate (IP) reaction, a selective method for visualization of phospholipids, was applied to the predentine and dentine of rat incisors and compared with malachite green aldehyde (MG) fixation/staining. Spot tests indicated (1) that IP specifically stains phospholipids, but not amino acids, displaying as do phospholipids, quaternary ammonium groups; and (2) phosphatidylserine and sphingomyelin were also stained by MGA. Although this reagent is known to interact with phosphorus, phosphoproteins remained unstained. In the rat incisor, an IP-positive network including granules and thin filaments was seen in predentine in the inter-collagen spaces, in many cases closely associated with collagen fibres and their periodic striations. In dentine, positively stained needle-like structures were located along individual collagen fibres, or at the surface of groups of collagen fibres. This staining pattern was unchanged on sections of material pretreated with acetone, whereas the staining was abolished or markedly reduced when the samples were treated either with chloroform/methanol or phospholipase C prior to the IP reaction. Pretreatment of the samples with hyaluronidase promoted subsequent diffusion of the staining. A very similar staining pattern was observed with MGA, in accordance with earlier reports. The present findings validate the histochemical results reported previously on the distribution and potential role(s) of phospholipids in dentine biomineralization.
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PMID:Iodoplatinate visualization of phospholipids in rat incisor predentine and dentine, compared with malachite green aldehyde. 751 28

A glycosaminoglycan (GAG) depolymerase that acts on chondroitin sulphate A (CS-A), chondroitin sulphate C (CS-C) and hyaluronic acid (HA) was purified to apparent homogeneity from a culture of Streptococcus intermedius, strain UNS 35, grown in minimal medium supplemented with CS-A as the sole carbon source. The enzyme was purified by ammonium sulphate precipitation followed by serial chromatography on DEAE Trisacryl M, CM Trisacryl M and heparin-agarose. SDS-PAGE analysis of the purified enzyme yielded a single band with a mol.wt of c. 83000. The purified GAG depolymerase was unusual in its substrate specificity. The enzyme was initially regarded as a CS depolymerase because of its induction by CS-A. However, the GAG depolymerase exhibited greatest activity against HA, whereas the degradation rates of CS-A and CS-C were c. 8% and 2%, respectively, of the rate with HA. On this basis the enzyme could be classified as a hyaluronidase rather than a CS depolymerase. The pH optimum was around neutrality and the enzyme was unusual in having a high pI of approximately 9.3.
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PMID:Purification and properties of a novel glycosaminoglycan depolymerase from Streptococcus intermedius strain UNS 35. 863 53

The vanadium is a metallic oligoelement present in the majority of tissues. Its abnormal biological disposal environment can be related with its possible teratogenicity and alteration in the contents of glycosaminoglycans acids (GAGs), which participate in the morphological processes and the maturation of Central Nervous System (CNS). The proposal of the project is to analyze the teratogenic effect of ammonium metavanadate (AMV) and its action on the GAGs in the CNS of the litter of albino rats. The ammonium metavanadate was diluted in distilled water in concentration of 100 and 200 ppm, drunk by the rats since their birth and/or weaning to adult age, except during the matching and gestation. The animals control drunk water without this metal. The litter were analyzed to detect possible congenital malformations, then CNS were removed of descendents and were processed by light microscope, cuts of 6 u were stained with H/E; Alcian Blue pH 3.5 and 5.6, this last one concentrations of C12Mg from 0.05 M to until 1.0 M. Previously parallels sections were treated with testicular hyaluronidase. The macroscopic analysis of the new born rats that came from rats that received AMV in concentrations 100 and 200 ppm, resulted in congenital anomalies like unilateral hypoplasia of olfactory bulbs and cerebral hemisphere. The microscopic analysis revealed changes in the layers patron of olfactory bulbs and an increased of alcianophilia in the pH 5.6 to 0.2 M MgC12, in the extracellular matrix of CNS of rats descendents treated with AMV to the dose 200 ppm, sensibles to the testicular hyaluronidase, corresponding to hyaluronic acid (HA) and chondroitin 4 and/or 6 sulphate (C4S or C6S) of low grade of sulphation. These results suggest that the AMV given to albino rats has a teratogenic result when it is used before the gestation and for long periods of animals life that alter the of GAGs of CNS contents during the development.
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PMID:[Teratogenic effects of ammonium metavanadate on the CNS of the offspring of albino rats. A histological and histochemical study]. 965 Apr 61

Enzyme inhibitory activities of 14 iridoids previously obtained from two Malaysian medicinal plants, Saprosma scortechinii and Rothmannia macrophylla, were evaluated in vitro using soybean lipoxygenase and bovine testis hyaluronidase. Most of the iridoids, including asperulosidic acid, paederosidic acid, and an epimeric mixture of gardenogenins A and B, did not show any effect on the enzyme activities, except for the bis-iridoids, which inhibited the lipoxygenase activity with their IC(50) values of approximately 1.3 times that of a known inhibitor, fisetin. Structural modification of asperulosidic acid and paederosidic acid through enzymatic hydrolysis by beta-glucosidase resulted in their inhibition towards the enzyme activities, and these activities were enhanced by the presence of some amino acids (lysine, leucine or glutamic acid) or ammonium acetate. Mixtures of gardenogenins A and B; isomers of non-glucosidic iridoids, incubated with amino acid or ammonium acetate did not show any inhibitory effect on the enzyme activities during the 6 h incubation period, except for lysine where spontaneous reaction between the iridoids and amino acid resulted in the inhibition of lipoxygenase activity. The results from these biomimetic reactions suggested that the iridoid aglycons and the intermediates formed by these reactive species could inhibit the enzyme activities, and thus substantiate previous reports that the formation of iridoidal aglycons is a prerequisite for the iridoid glycosides to demonstrate some of the biological activities. In addition, the results also indicated that it is worthwhile to further explore these intermediates as potential anti-inflammatory agents.
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PMID:Effects of iridoids on lipoxygenase and hyaluronidase activities and their activation by beta-glucosidase in the presence of amino acids. 1261 46

A new method for the identification of oligosaccharides obtained by enzymatic digestion of hyaluronic acid (HA) with bacterial hyaluronidase (HA lyase, E.C. 4.2.2.1, from Streptococcus agalactiae) using online capillary electrophoresis/electrospray mass spectrometry (CE/ESI-MS) is presented. A fused-silica capillary coated with polyacrylamide was used with a 40 mM ammonium acetate buffer at pH 9.0 and a separation voltage of +30 kV applied to the inlet. Separation was achieved for oligosaccharides containing 4-16 monomers. The migration behavior follows the chain length of the oligomers, regardless of charge state. However, no linear relationship was found for the relation between mobility and chain length. Using an ion trap mass analyzer, complementary structural information was obtained by MS/MS and MS(n) experiments.
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PMID:Identification of hyaluronic acid oligosaccharides by direct coupling of capillary electrophoresis with electrospray ion trap mass spectrometry. 1262 20

Poly(L-lysine)/hyaluronan (PLL/HA) films were chemically cross-linked with a water soluble carbodiimide (EDC) in combination with a N-hydroxysulfo-succinimide (NHS) to induce amide formation. Fourier transform infrared spectroscopy confirms the conversion of carboxylate and ammonium groups into amide bonds. Quartz crystal microbalance-dissipation reveals that the cross linking reaction is accompanied by a change in the viscoelastic properties of the films leading to more rigid films. After the cross-linking reaction, both positively and negatively ending films exhibit a negative zeta potential. It is shown by fluorescence recovery after photobleaching measured by confocal laser scanning microscopy that cross-linking dramatically reduces the diffusion of the PLL chains in the network. Cross linking also renders the films highly resistant to hyaluronidase, an enzyme that naturally degrades hyaluronan. Finally, the adhesion of chondrosarcoma cells on the films terminating either with PLL or HA is also investigated. Whereas the non cross-linked films are highly resistant to cell adhesion, the cells adhere and spread well on the cross-linked films.
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PMID:Improvement of stability and cell adhesion properties of polyelectrolyte multilayer films by chemical cross-linking. 1500 86

The endodontium and periodontium are closely related and disease of one may lead to secondary disease in the other. The differential diagnosis of endodontic and periodontal disease is of vital importance, so that the appropriate treatment can be done. Microorganisms play a primary role in endodontic and periodontal infections. The magnitude of the host response will be directly proportional to the virulence and the number of microbial cells present. Tissue damage caused by bacteria is mediated by either direct or indirect mechanisms. Direct harmful effects caused by bacteria involve their products, such as enzymes (collagenase, hyaluronidase, condroitinase, acid phosphatase), exotoxins and metabolites (bytrate, propionate, ammonium polyamines, sulphured compounds). In addition, bacterial components such as peptidoglycan, teichoic acid, fimbriae, outer membrane proteins, capsule, and lypopolysaccharide, stimulate the development of host immune reaction capable of causing severe tissue destruction.
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PMID:Etiological findings in endodontic-periodontal infections. 1562 83


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