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

The use of a hyaluronic acid-binding proteoglycan (hyaluronectin) as a probe for the detection of hyaluronic acid has facilitated the development of an indirect enzymo-immunological assay for hyaluronidase. Plastic microtest ELISA plates were coated with hyaluronic acid. Incubation with hyaluronidase led to the destruction of insolubilized hyaluronic acid in proportion to the hyaluronidase concentration of samples. Residual hyaluronic acid was assayed by its capacity to bind immune complexes made up of hyaluronectin supplemented with alkaline phosphatase-conjugated anti-hyaluronectin antibodies. The technique was very sensitive and permitted the detection of as little as 10(-10) NFU of bovine testicular hyaluronidase. Hyaluronidase was detected by this technique in human sera, bee venom and culture medium of human hepatoma cell lines.
 ...
PMID:An indirect enzymoimmunological assay for hyaluronidase. 331 96

A study was made of hyaluronidase in ram semen. The end-group assay conditions used to determine activity quantitatively were chosen to ensure reliability as well as sensitivity [Gacesa, Savitsky, Dodgson & Olavesen (1981) Anal. Biochem. 118, 76-84]; they led to 1 W.H.O. Standard International Hyaluronidase Unit displaying 0.1263 EC munit (1 EC unit of activity releases 1 mumol equivalent of N-acetylglucosamine end groups/min at 37 degrees C). All the activity in the semen was shown to be sperm-derived, and intact spermatozoa were estimated to contain 1.23 EC units per 10(9) cells. In a low-ionic-strength medium, only some 20% of the hyaluronidase was extractable, although up to 80% of the activity could be extracted as the ionic strength was increased; further addition of detergent extracted the remainder. During purification of the enzyme, it was found that inclusion of poly(vinyl alcohol) in the media stabilized the activity; detergent inclusion also improved the yield, especially during early stages. As a consequence both of reliable quantitative determination and of stabilization, a number of forms of hyaluronidase could be isolated in high yield, by using anion-exchange chromatography, cation-exchange chromatography, affinity chromatography and gel filtration. The existence of all these forms was confirmed by electrophoresis and immunoblotting with the use of a monoclonal anti-(ram hyaluronidase) antibody, and their presence in very freshly prepared sperm extracts was demonstrated. The specific activity of the isolated major hyaluronidase form was 15.0 EC units/mg; this was equivalent to 119,000 W.H.O. units/mg, higher than any other previously reported values.
 ...
PMID:Hyaluronidase in ram semen. Quantitative determination, and isolation of multiple forms. 342 26

Treatment of arthritic synovial fluid with hyaluronidase reduced the recovery of mononuclear cells as well as their in vitro IgA and IgG synthesis. Hyaluronidase should be avoided in the treatment of synovial fluid when unselected mononuclear cell populations are required.
 ...
PMID:Hyaluronidase treatment of synovial fluid affects the recovery of mononuclear cells and their in vitro immunoglobulin synthesis. 342 39

In 27 patients with squamous cell carcinomas of the head and neck region hyaluronidase was added to cytostatic chemotherapy, in part of them from the beginning and in part after development of chemoresistance. We administered either ampoules containing 750 i. u. of Permease in a dosage between 7,500 i. u. and 22,500 i. u., or alternatively a preparation of hyaluronidase containing 200,000 i. u. Hyaluronidase was well tolerated; there were reversible allergic reactions in only 2 patients. We obtained CR 14/27, PR 5/27, NC 3/27. After giving hyaluronidase to chemoresistant patients CR 8/16, PR 3/16 and NC 3/16 were achieved. The course of the disease in chemoresistant cases make it probable that hyaluronidase can improve the prognosis in these patients. With regard to the kind of activity it seems noteworthy that the amount of mucopolysaccharides is increased in many malignancies; furthermore, the transport of cytostatic agents to the tumour cells can be improved.
 ...
PMID:[Hyaluronidase in cytostatic therapy of ENT tumors]. 360 Jan 26

The process of lens regeneration in newts involves the dedifferentiation of pigmented iris epithelial cells and their subsequent conversion into lens fibers. In vivo this cell-type conversion is restricted to the dorsal region of the iris. We have examined the patterns of hyaluronate accumulation and endogenous hyaluronidase activity in the newt iris during the course of lens regeneration in vivo. Accumulation of newly synthesized hyaluronate was estimated from the uptake of [3H]glucosamine into cetylpyridinium chloride-precipitable material that was sensitive to Streptomyces hyaluronidase. Endogenous hyaluronidase activity was determined from the quantity of reducing N-acetylhexosamine released upon incubation of iris tissue extract with exogenous hyaluronate substrate. We found that incorporation of label into hyaluronate was consistently higher in the regeneration-activated irises of lentectomized eyes than in control irises from sham-operated eyes. Hyaluronate labeling was higher in the dorsal (lens-forming) region of the iris than in ventral (non-lens-forming) iris tissue during the regeneration process. Label accumulation into hyaluronate was maximum between 10 and 15 days after lentectomy, the period of most pronounced dedifferentiation in the dorsal iris epithelium. Both normal and regenerating irises demonstrated a high level of endogenous hyaluronidase activity with a pH optimum of 3.5-4.0. Hyaluronidase activity was 1.7 to 2 times higher in dorsal iris tissue than in ventral irises both prior to lentectomy and throughout the regeneration process. We suggest that enhanced hyaluronate accumulation may facilitate the dedifferentiation of iris epithelial cells in the dorsal iris and prevent precocious withdrawal from the cell cycle. The high level of hyaluronidase activity in the dorsal iris may promote the turnover and remodeling of extracellular matrix components required for cell-type conversion.
 ...
PMID:Hyaluronic acid production and hyaluronidase activity in the newt iris during lens regeneration. 365 53

Hyaluronidase was purified to apparent homogeneity from the spent medium of Peptostreptococcus sp. strain 84H14S. The enzyme was purified 310-fold by ethanol precipitation, gel chromatography, and cation-exchange chromatography with a recovery of 42% of the original activity in the culture medium. The molecular weight of the purified enzyme was estimated to be 160,000 by gel filtration with Sephacryl S-300. Like bacterial mucopolysaccharidases of other sources, the enzyme carried out an eliminative reaction with the substrate, producing 4,5-unsaturated disaccharides as the final end products. Its optimum temperature of activity is 46 degrees C. The purified peptostreptococcal hyaluronidase was different from previously reported bacterial hyaluronidases in several respects. It degraded hyaluronic acid rapidly and also exhibited some activity against chondroitin sulfate A and chondroitin sulfate C. The KmS for hyaluronic acid, chondroitin sulfate A, and chondroitin sulfate C were 0.14, 1.4, and 2.6 mg/ml, respectively. The specific activity of hyaluronidase was much higher than that of any previously purified mucopolysaccharidases. The Vmax against hyaluronic acid reached 400 mmol of product per min per mg of protein at 22 degrees C. The peptostreptococcal hyaluronidase was also unique in that its optimum pH of activity was around neutrality, whereas other bacterial hyaluronidases were most active at acidic pHs.
 ...
PMID:Purification and characterization of hyaluronidase from oral Peptostreptococcus species. 388 52

Hyaluronidase treatment of mouse oligodendroglioma cells in monolayer culture resulted in a 4-5-fold stimulation of hyaluronate synthetase, assayed in washed membrane preparations [Philipson, L., & Schwartz, N. B. (1984) J. Biol. Chem. 259, 5017-5023]. We now report studies on the mechanism of the hyaluronidase-induced increase in the specific activity of the membrane-bound synthetase complex. The stimulation was dependent on the concentration of hyaluronidase but not on the particular bond cleaved or the nature of the product generated. Analysis of chain growth during cell-free synthesis by the disaccharide ratio method suggested that substantial internal labeling of hyaluronate chains had occurred. With both treated and untreated membranes, greater than 90% of incorporated (and recovered) radioactivity appeared in unsaturated disaccharides. Further analysis showed that hyaluronidase treatment increased both the rate of elongation and the rate of release of elongated chains from the enzyme complex. Hyaluronidase treatment also caused a change in the apparent steady-state kinetic patterns of double-reciprocal plots from intersecting lines for membranes from control cells to a family of parallel lines. Both the overall stimulation of synthesis and the change in apparent kinetic pattern were reversed by brief incubation of washed cells in the absence of hyaluronidase. These results have led to the development of an explicit kinetic model for hyaluronate synthesis which suggests an explanation for the switch in apparent kinetic patterns based on changing concentrations of a postulated key intermediate.
 ...
PMID:Effect of hyaluronidase treatment of intact cells on hyaluronate synthetase activity. 393 51

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.
 ...
PMID:[Purification and properties of staphylococcal hyaluronidase]. 396 93

Hyaluronidase (hyaluronate 4-glycanohydrolase, EC 3.2.1.35) has been isolated from pig liver and purified 1720-fold with an overall yield of 9.5%. The enzyme was purified using an acid-extraction technique followed by successive chromatography on DEAE-cellulose, two boronate affinity columns and Sephadex G-75. This final preparation, which was essentially homogeneous as determined by gel electrophoresis, was a single subunit enzyme of apparent molecular weight 70 000 with an isoelectric point of 5.0. No contaminant enzymes capable of degrading glycosaminoglycans could be detected in the final preparation. The substrate specificity of the enzyme was the same as for bovine testicular hyaluronidase; however, both the Km and V values were significantly lower for the pig liver enzyme with all of the substrates tested (hyaluronate, chondroitin 4-sulphate, chondroitin 6-sulphate). A full kinetic analysis of the enzyme using hyaluronate as a substrate showed that the activity of pig liver hyaluronidase was uncompetitively activated by either protons or NaCl.
 ...
PMID:The purification and some properties of pig liver hyaluronidase. 397 Sep 70

Cultured myoblasts were found to exhibit extensive, Streptomyces hyaluronidase-sensitive pericellular coats as revealed by exclusion of particles (fixed red blood cells). These coats are not discernible subsequent to fusion of the myoblasts to form myotubes. The myoblasts contained 2.5 times more hyaluronate attached to their cell surface than myotubes when the data was expressed per unit of protein, but no change in hyaluronate was evident on a per DNA basis. Hyaluronidase activities in the cultures were equivalent when expressed per unit of protein. We conclude that, although the myotubes accumulate larger amounts of protein than myoblasts, there is no compensatory increase in hyaluronate.
 ...
PMID:Loss of hyaluronate-dependent coat during myoblast fusion. 397 68


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>