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)

Experiments were performed to indentify the series elastic component (SEC) in intact dog carotid artery held at in situ length. The vessels were studied during excitation of the muscle with norepinephrine and after metabolic poisoning with potassium cyanide and sodium iodoacetate. Static circumferential stress-strain curves and stress-quick-release stiffness curves were examined to evaluate Maxwell and Voigt model elements. The vessels were studied at 33, 36, and 39 degrees C. Temperature variations altered active stress, but did not alter connective tissue properties or the Maxwell SEC stiffness. The Voigt model SEC stiffness was altered, but this was secondary to changes in active stress. Thus, most of the SEC is separate from the contractile apparatus. Other vessels were treated with elastase, collagenase, or hyaluronidase to digest the connective tissue components of the wall. Hyaluronidase had no effect on mechanics. Elastase and collagenase altered connective tissue properties, but only elastase unequivocally altered SEC stiffness. This analysis indicated 1) that the carotid artery wall is better represented by a Maxwell model than a Voigt model, and 2) that the SEC in intact carotid artery is primarily elastin.
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PMID:Identification of smooth muscle series elastic component in intact carotid artery. 19 Aug 98

When normal or SV40-transformed Balb/c 3T3 cells are treated with the Ca++-specific chelator EGTA, they round up and pull away from their footpad adhesion sites to the serum-coated tissue culture substrate, as shown by scanning electron microscope studies. Elastic membranous retraction fibers break upon culture agitation, leaving adhesion sites as substrate-attached material (SAM) (Cells leave "footprints" of substrate adhesion sites during movement by a very similar process.) SAM contains 1-2% of the cell's total protein and phospholipid content and 5-10% of its glucosamine-radiolabeled polysaccharide, most of which is glycosaminoglycan (GAG). By one- and two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis, there is considerable enrichment in SAM for specific GAGs; for the glycoprotein fibronectin; and for the cytoskeletal proteins actin, myosin, and the subunit protein of the 10 nm-diameter filaments. Fibrillar fibronectin of cellular origin and substratum-bound fibronectin of serum origin (cold-insoluble globulin, CIg) have been visualized by immunofluorescence microscopy. The GAG composition in SAM has been examined under different cellular growth and attachment conditions. Heparan sulfate content correlates with glycopeptide content (derived from glycoprotein). Newly attaching cells deposit SAM with principally heparan sulfate and fibronectin and little of the other GAGs. Hyaluronate and chrondroitin proteoglycans are coordinately deposited in SAM as cells begin spreading and movement over the substrate. Cells attaching to serum-coated or CIg-coated substrates deposited SAM with identical compositions. The proteoglycan nature of the GAGs in SAM has been examined, as well as the ability of proteoglycans to form two classes of reversibly dissociable "supramolecular complexes" - one class with heparan sulfate and glycopeptide-containing material and the second with hyaluronate-chondroitin complexes. Enzymatic digestion of "intact" SAM with trypsin or testicular hyaluronidase indicates that (1) only a small portion of long-term radiolabeled fibronectin and cyto-skeletal protein is bound to the substrate via hyaluronate or chondroitin classes of GAG; (2) most of the fibronectin, cytoskeletal protein and heparan sulfate coordinately resist solubilization; and (3) newly synthesized fibronectin, which is metabolically labile in SAM, is linked to SAM by hyaluronate- and/or chondroitin-dependent binding. All of our studies indicate that heparan sulfate is a direct mediator of adhesion of cells to the substrate, possibly by binding to both cell-surface fibronectin and substrate-bound CIg in the serum coating; hyaluronate-chondroitin complexes in SAM appear to be most important in motility of cells by binding and labilizing fibronectin at the periphery of footpad adhesions, with subsequent cytoskeletal disorganization.
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PMID:Fibronectin and proteoglycans as determinants of cell-substratum adhesion. 23 21

Hyaluronidase from bull sperm was fractionated by ammonium sulfate and further purified by DEAE-cellulose and Sephadex chromatography. The highly purified hyaluronidase preparation showed 2,370 units per mg of protein (68,730 N.F. units per mg of protein), i.e. 182-fold purification. Disc gel electrophoresis showed one major component. The molecular weight of bull sperm hyaluronidase was 62,000 by sodium dodecyl sulfate gel electrophoresis. Hyaluronidase from bull sperm has optimum activity at pH 3.8 and an absolute requirement for cations. Kplus and Naplus have a greater effect than Ca2plus, Mg2plus, and Mn2plus, whereas Co2plus, Cu2plus, and Zn2plus do not affect the enzyme activity. Purified preparations are less stable than crude extracts stored frozen at minus 15 degrees. Km of hyaluronidase with hyaluronic acid as substrate is 3.7 mg per ml and Vmax is 2.4 mumol per min by Hofstee plot.
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PMID:Purification and properties of hyaluronidase from bull sperm. 23 95

Two new allergenic specificites were detected in honeybee venom and the two corresponding protein substances isolated by gel filtration, immunoadsorption, and ion exchange chromatography. The first of these, allergen B, has a molecular weight ranging from 49,000 to more than 200,00 d and can be recognized by rabbit and guinea pig antisera as well as by human reaginic sera using the radioallergosorbent test (RAST). Allergen B gives a single line in immunodiffusion distinct from hyaluronidase, phospholipase A, melittin, and the other high molecular weight substances described and gives a single band at 49,000 d in sodium dodecyl sulfate (SDS) polyacrylamide gel. The second substance, allergen C, has a molecular weight of 105,000 d and was separated from allergen B by immunoadsorption with insoluble antibody. Allergen C was shown to be distinct from the other sustances in bee venom by immunodiffusion with animal antisera. One human reaginic serum was monospecific for allergen C. Two other minor components of 86,000 and 71,000 d are present in bee venom; their allergenic activities are unknown. The two specifities, B and C, comprise most of the reactivity of the previously described Sephadex G-75 fraction 1 and clearly are important allergens, reacting with 98% of sera from bee venom-allergic individuals.
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PMID:Allergens in bee venom II. Two new high molecular weight allergenic specificities. 40 40

Early membrane events in erythroid differentiation were investigated by means of cell electrophoresis utilizing cultured Friend erythroleukemia cell clones of different inducibility. The cell electrophoretic mobility decreased by 18% within 30 min of treatment with 1.5% dimethyl sulfoxide (DMSO) in highly inducible clones but not in noninducible clones. The reduced mobility persisted for 5 days of incubation with DMSO until hemoglobin synthesis. DMSO treatment for less than 16 hr and subsequent incubation without the drug resulted in the complete recovery of the mobility and no hemoglobin synthesis. Longer exposure to DMSO resulted in the loss of recovery of mobility and an increasing fraction of benzidine-positive cells seen on Day 5. Measurement of the electrophoretic mobility after the removal of acidic sugars by their specific enzymes suggested that hyaluronidase-sensitive negative charges were lost from the cell surface only in highly inducible clones. The mobility reduction associated with hyaluronic acid was also caused by other potent inducers (sodium butyrate, N-methylacetamide, and N,N-dimethylacetamide). These results suggest that the decrease in cell surface glycocalyx might be an early step in the induction of differentiation of Friend erythroleukemia cells.
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PMID:Early decrease in hyaluronidase-sensitive cell surface charge during the differentiation of Friend erythroleukemic cells by dimethyl sulfoxide. 42 53

Chondroitinase B and chondroitinase C were separated from an extract of Flavobacterium heparinum induced with chondroitin 6-sulfate by using column chromatography on hydroxylapatite. Chondroitinase C was eluted together with the activities of hyaluronidase, delta4,5glycosiduronase, and sulfatase. The latter two activities were eliminated exclusively by passing the crude chondroitinase C fraction through a phosphono-cellulose column pre-equilibrated with 0.07M sodium phosphate buffer (pH 6.8). Chondroitinase C was then purified by affinity chromatography using dermatan sulfate-bound AH-Sepharose 4B coated with the same glycosaminoglycan. Purification of the enzyme was achieved 18-fold and in 73% yield. On the other hand, the activities of delta4,5glycosiduronase and sulfatase were decreased to 50 and 60%, respectively, as compared with those in the crude chondroitinase B fraction, after passing the fraction through a column of phosphono-cellulose pre-equilibrated with 0.1M sodium phosphate buffer (pH 6.8). The remaining activities of these two enzymes were then eliminated from chondroitinase B by affinity chromatography with heparin-bound AH-Sepharose 4B coated with dermatan sulfate. In the affinity chromatography used in the present study, non-covalent coating of the glycosaminoglycan-bound (covalently) AH-Sepharose 4B with the same or another glycosaminoglycan was found to be important.
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PMID:Purification of chondroitinase B and chondroitinase C using glycosaminoglycan-bound AH-Sepharose 4B. 42 37

Oligomers of hyaluronic acid were prepared by digestion of hyaluronic acid from rooster combs with testicular hyaluronidase (hyaluronate 4-glycanohydrolase, EC 3.2.1.35), leech head hyaluronidase (hyaluronate 3-glycanohydrolase, EC 3.2.1.36), and with fungal hyaluronidase (hyaluronate lyase from Streptomyces hyalurolyticus). The oligomers were fractionated by gel permeation, using Sephadex G-50. Oligomers isolated after incubation of the hyaluronic acid with the testicular hyaluronidase were further modified. To prepare oligomers with N-acetylglucosamine at both ends, terminal nonreducing glucuronic acid residues were removed with beta-glucuronidase. Reducing terminal N-acetylglucosamine residues were removed by reaction under mildly alkaline conditions. The reducing terminal N-acetylglucosamine residues were also reduced with sodium borohydride to form N-acetylglucosaminitol. The potentials of the various oligosaccharides to bind to the proteoglycan from bovine nasal septum cartilage were estimated by determining their effectiveness as inhibitors of the proteoglycan-hyaluronate interaction. The present study shows that, to bind maximally to the proteoglycan, the hyaluronate oligosaccharide must be at least 10 sugar residues in length and be terminated at the nonreducing and reducing ends with a glucuronate residue and an N-acetylglucosamine residue, respectively. Sugar residues extended beyond this basic decasaccharide, do not interact with the hyaluronate binding site on the proteoglycan.
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PMID:Interactions of cartilage proteoglycans with hyaluronate. Inhibition of the interaction by modified oligomers of hyaluronate. 43 8

Anionic sites on the surface of Brucella canis were visualized in the electron microscope by staining with positively charged ferric oxide hydrosols in acetic acid (AI-reagent), or propanoic acid (PI-reagent), and with a polycationic ferritin derivative. With the AI-reagent, single or small aggregates of ferric oxide particles were bound to the cell surface of Br. canis, whereas, with the lipophilic PI-reagent, the microorganisms were heavily stained with focal aggregates of iron granules. The polycationic ferritin label was uniformly distributed over the entire cell surface of Br. canis. The ferritin label was not bound on the surface of the organisms after prior treatment with trichloroacetic acid or methanolic hydrochloric acid. Treatment with aqueous acetone, chloroform/methanol, diethyl ether, sodium deoxycholate, pronase, lysozyme, hyaluronidase, and sodium periodate neither influenced the morphology of the Brucella nor diminished their ionic binding sites. Our results indicate that the anionic sites on the cell surface of Br. canis may be carboxyl and phosphate groups of lipopolysaccharides.
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PMID:[Ultrastructural investigations on anionic surface sites of Brucella canis (author's transl)]. 60 17

Cauda epididymal sperm of mature guinea pigs were incubated (37 degrees, 5% CO2 in air). 10% of the total enzyme activity was released into the medium in 4 hr, 30% in 24 hr. Addition of lysolecithin resulted in rapid release of hyaluronidase. Vitamin C (0.54 mM), sodium fluoride (0.02 M), and cholesterol increased the rate of release whereas citrate (20 mM) diminished it. No effect upon hyaluronidase release was noted upon addition of KCN (10(-2)M), progesterone (250 microgram/ml), testosterone (500 microgram/ml), spermine (1.15 mg/ml), inositol (5.6 mM), or chloroquine phosphate (0.54 mM).
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PMID:Hyaluronidase release from guinea pig spermatozoa as affected by reproductive tract secretions and metabolic inhibitors. 73 70

Potassium chloride (KCl) given subcutaneously in high concentrations causes necrosis of skin, possibly from vasoconstriction around the injection site. The authors studied guinea pigs given subcutaneous injections of various volumes and concentrations of KCl and observed the severity of the cutaneous lesions. In further experiments, therapeutic agents were injected subcutaneously 10 minutes after KCl infiltration. The severity of cutaneous lesions was not affected by various volumes of KCl of the same concentration, but was correlated positively with increasing concentrations of the salt when concentration was varied. Dextrose, 5%, and sodium bicarbonate, 1 M, had no effect on the cutaneous lesions caused by KCl, while hyaluronidase, 150 U/ml, lessened them. Lidocaine, 1%, a vasodilator, eliminated cutaneous lesions caused by KCl. Kcl-induced lesions may be due to vasocontriction, which can be relieved by lidocaine.
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PMID:Lidocaine treatment of experimental cutaneous lesions from potassium chloride injection. 91 Oct 51


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