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)

Hyaluronic acid (4 mg/ml) augmented elevenfold the copper-catalyzed (7 muM) thermal (63 degrees C, 2 hours) aggregation of human gamma globulin (2 mg/ml) in 0.075 M phosphate buffer, pH 7.4. Almost no augmentation of aggregation occurred with hyaluronidase-treated hyaluronate. Hyaluronate-augmented copper-catalyzed thermal aggregation was inhibited by L-histidine, gold thiomalate, N-ethylmaleimide, p-chloromercuribenzoic acid, and ethylenediaminetetraacetic acid. Together with previous reports of a decreased blood histidine concentration in rheumatoid arthritis, these studies provide a possible explanation for the affinity of this disease for joints.
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PMID:Sulfhydryl-dependent thermal aggregation of human gamma globulin: augmentation by hyaluronic acid. 4 54

Hyaluronidase activity of human endometrial tissues and uterine fluids was investigated. Endometrial tissue and uterine fluid specimens were obtained from normal human subjects, and different cases of uterine dysfunction induced by steroidal contraceptives, copper IUD, lactational amenorrhea, and in early pregnancy. Hyaluronidase activity was found to increase from Cycle Days 8 to 10 and reach the maximum value during the secretory phase. Hyaluronidase activity was reduced in both endometrial tissue and uterine fluid during lactational amenorrhea and early pregnancy, and was drastically reduced in copper-IUD and steroidal contraceptive users. The low hyaluronidase activity in the early phase of the cycle may be due to rapid growth of endometrial tissue. In the secretory phase, the corresponding activities were found to increase because of high secretory activity and enhanced catabolic processes. In early pregnancy, the low lysosomal enzyme activity may also be explained on the basis of increased endometrium tissue growth. Low hyaluronidase activity of amenorrhic subjects may be due to the absence of ovarian steroids.
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PMID:Hyaluronidase activity of human endometrial tissues & uterine fluids. 121 11

1. A marine hyaluronidase was purified 261-fold from the stonefish (Synanceja horrida) crude venom using Sephacryl S-200 HR and heparin affinity-gel chromatography. 2. Stonefish hyaluronidase has a pI of 9.2, a mol. wt of 62,000 and it was purified to a very high spec. act. of 1.6 x 10(6) NFU/mg protein. 3. It was heat sensitive and was inhibited by Cu2+, Hg2+ and heparin. 4. Stonefish hyaluronidase did not contain any haemorrhagic or lethal activity. 5. The N-terminal sequence of stonefish hyaluronidase has been determined to be A-P-S-X-D-E-G-N-K-K-A-D-N-L-L-V-K-K-I-N.
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PMID:Purification and partial characterization of hyaluronidase from stonefish (Synanceja horrida) venom. 149 62

Many drugs have been reported to interfere with copper-reduction or glucose oxidase tests used to measure urine glucose. However, only a few drugs or drug classes have been well documented to clinically interfere with these tests. The interfering drugs include ascorbic acid, beta-lactam antibiotics (e.g., cephalosporins and penicillins), levodopa, and salicylates. Several other drugs may also interfere with certain urine glucose tests, but the interactions are poorly documented. These drugs include chloral hydrate, hyaluronidase, nalidixic acid, nitrofurantoin, p-aminosalicylic acid, phenazopyridine, probenecid, and X-ray contrast media. Drugs or their metabolites that are strong reducing substances produce false-positive results by the copper-reduction method and false-negative results by the glucose oxidase method. The beta-lactam antibiotics interfere with copper-reduction tests by producing copper compounds of various colors that confuse interpretation of test results. Tables are provided that summarize the drug interferences discussed.
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PMID:Review of drug interference with urine glucose tests. 355 7

Microbial hyaluronidase (EC 4.2.2.1) was isolated from the culture fluid of Staphylococcus aureus 0-15 with purification by precipitation with 1 volume of ethyl alcohol, chromatography on DEAE cellulose and ultrafiltration through DA type membranes with the pore size of 0.65 micron ("Millipore") and PM-10 membranes ("Amicon"). The specific activity of the enzyme averaged to 2700 turbidimetric units or 32130 IU. 6585-fold purification of the enzyme was performed. The optimum action on hyaluronic acid was observed at pH 5.0-6.5. Hyaluronidase was inhibited by Fe3+, Fe2+ and Cu2+, activated by Ca2+ and stabilized by 0.15 M NaCl. It was detected that the enzyme had two molecular forms with the isoelectric points of 5.4 and 6.5 and the molecular weights of 55 000 and 24 0000 D respectively. The glycoprotein nature of the enzyme was shown. The immobilized form of hyaluronidase on activated polyglucin, a soluble biocompatible polymer was prepared. The form is characterized by higher thermostability.
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PMID:[Purification and properties of staphylococcal hyaluronidase]. 396 93

Stable, transparent gels can be prepared from hyaluronate solutions by adding CuSO4. The best gelation was found using solutions of 2 mg/ml hyaluronate in glass-distilled water at a pH of 6.2 after the addition of 1 mg/ml CuSO4. Methylation of the carboxyl groups of the hyaluronate completely abolished the gelation, indicating the importance of the carboxyl groups for the gel formation with Cu2+ ions. Gelation also depends on the molecular size of the hyaluronate, since hyaluronate was not able to form a gel after depolymerization with hyaluronidase.
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PMID:Preparation of gels from hyaluronate solutions. 712 7

A hyaluronidase (EC 3.2.1. 35) was isolated and purified from Agkistrodon acutus venom. The purification procedure included CM-Sephadex C-50 chromatography, gel-filtration on Sephadex G-75 and CM-Sephadex C-25 chromatography. The purified preparation of the enzyme was homogeneous on polyacrylamide gel electrophoresis at pH 4.3, a 45-fold purification being obtained. The hyaluronidase was a glycoprotein (positive PAS staining) with a molecular weight of 33,000 and a pI of 10.3. No hemorrhagic activity was found. The hyaluronidase had an optimum pH of 3.5-5.0 and an optimum temperature of 37 degrees C. It was heat sensitive, was more stable in the acidic than in the neutral region, and lost its activity in the alkaline region. Fe2+, Cu2+ and heparin inhibited the venom hyaluronidase. The Km value for hyaluronic acid was 6.2 X 10(-3) mg/ml.
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PMID:Purification and partial characterization of hyaluronidase from five pace snake (Agkistrodon acutus) venom. 716 13

The gingiva of rat molars was studied at the light microscope level using glutaraldehyde as fixative, Cuprolinic Blue for visualizing polyanionic glycosaminoglycans and the autometallographic technique for enhancing the copper signal of the cationic dye. The polyanions were located inside the epithelial cells in the junctional epithelium, whereas a network located along either the plasma membrane or the intercellular spaces, or both, of the gingival oral epithelium and sulcular oral epithelium was evident with autometallography. In these cases, positive staining was limited to the basal and spinous layers, the granular and keratinized layers being unstained. With the transmission electron microscope, electron-dense aggregates were seen in the gingival lamina propria, in the basement membrane and along the plasma membrane of the keratinocytes of the basal and spinous layers of the gingival and sulcular oral epithelia. In the junctional epithelium, Cuprolinic Blue-positive granules, 25 nm in diameter, were seen in the cytoplasm. Together with some vesicles containing electron-dense material, they may account for the staining process noted after autometallography. When the ultra-thin sections were digested with bovine testicular hyaluronidase, the staining was abolished. This indicates that glycosaminoglycans were primarily responsible for the staining pattern visualized with these methods. In the junctional epithelium, the cytosolic location of the 25 nm granules reflects either transcellular transfer between the plasma membrane and the nucleus or accumulation of glycosaminoglycans in this group of keratinocytes. The glycoconjugates located inside vesicles or vacuoles are related to endocytosis and lysosomal degradation. Interstitial glycosaminoglycans seen in the two types of oral epithelium may play a role in the diffusion of water and nutriments.
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PMID:Cuprolinic blue visualization of cytosolic and membrane-associated glycosaminoglycans in the rat junctional epithelium and gingival epithelia. 751 65

Enzymatic degradation of hyaluronan (HA) by testicular hyaluronidase (HAase, hyaluronate 4-glucanohydrolase) requires inclusion of mono- or divalent cations in the reaction mixture. Most divalent cations activated HAase with equal potency; however, Cu2+ suppressed degradation, and Ca2+ showed a concentration-dependent regulation of size of the oligosaccharide products. Careful selection of HAase assay parameters is critical for discovery of novel HAase inhibitors and for preparation of controlled-size oligosaccharide fragments.
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PMID:Control of enzymatic degradation of hyaluronan by divalent cations. 1051 49

The trichostrongylid nematode Haemonchus contortus released a hyaluronic acid-degrading enzyme during in vitro development from the third (L3) to fourth (L4) larval stage. The enzyme did not degrade chondroitin sulfate A. Enzyme activity was optimal between pH 4.0 and 6.0, and the enzyme was inhibited by high concentrations of NaCl; the divalent cations Cu2+, Zn2+, Ca2+, and Mn2+ were not inhibitory. The hyaluronidase had a molecular mass estimated at 57 kDa by sucrose density gradient centrifugation and at 111 kDa by substrate sodium dodecyl sulfate polyacrylamide gel electrophoresis (reducing and nonreducing conditions), suggesting the formation of a dimer during the electrophoretic separation conditions. The level of hyaluronidase released during in vitro development peaked between 24 and 48 hr in culture and then gradually decreased, with little or no activity present in the 168-hr culture fluid. The enzyme was not detected in culture fluid from 24-hr incubations of either the mid-L4 stage (obtained from sheep 7 days postinfection) or the adult stage (obtained from sheep 30-35 days postinfection). The temporal expression of the hyaluronidase suggested a role for this enzyme in the early stages of the L3-L4 developmental process.
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PMID:A developmentally regulated hyaluronidase of Haemonchus contortus. 1112 10


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