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)

Acrosin and acrosomal hyaluronidase were inhibited by tetradecyl sodium sulphate (TDSS) in vitro at concentrations of less than 10(-4) M. TDSS prevented the removal in vitro of the cumulus oophorus by testicular hyaluronidase and the zona pellucida by acrosin. TDSS had a contraceptive effect in rabbits when administered intravaginally before coitus or released at levels of 1-3 micrograms/day from intrauterine silicone rubber devices.
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PMID:Antifertility effects of tetradecyl sodium sulphate in rabbits. 634 64

A study was designed to determine whether tetradecyl sodium sulfate (TDSS), a potent inhibitor of both acrosin and hyaluronidase, would have a contraceptive effect in rabbits when a controlled level of TDSS was released from a vaginal delivery system over a 4-week period. The toroidal shaped delivery system was composed of a core of TDSS incorporated in polyurethane surrounded by a rate-limiting membrane of polyurethane. These devices were found to have a sustained in vitro TDSS release rate of equal to or greater than 400 mcg/day for over 30 days and had a complete contraceptive effect in 15 rabbits bred weekly for 4 weeks. No toxic effects were noted at 20 mg/day doses, but slight to moderate vaginal irritation was observed in the 50 and 100 mg/day groups. These results clearly demonstrate that TDSS is a useful intravaginal contraceptive agent when incorporated in a delivery system that continuously releases the compound into the vagina. 175 corpora lutea were found in the ovaries of the study rabbits, indicating that TDSS has no effect on ovulation. It remains unknown whether the TDSS binds to all the spermatozoa at the point of TDSS release in the vagina or whether some TDSS finds its way into the oviduct after release into the vagina and finally binds there to the few spermatozoa that reach this site. The vaginal delivery system shown in this study to be efficacious in rabbits could lead to the development of a similar device for human contraception. The advantages of this system are that it frees users from daily or postcoital administration, is capable of self-insertion, and uses a nonhormonal agent as the active ingredient.
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PMID:An intravaginal contraceptive device for the delivery of an acrosin and hyaluronidase inhibitor. 636 1

Histochemical procedures for the mouse sperm enzymes hyaluronidase, esterase and acrosin were used to test the inhibitory effects of the low molecular weight hyaluronidase inhibitor sodium aurothiomalate (Myocrisin): hyaluronidase and esterase, but not acrosin, were inhibited. These enzymes were also inhibited in testis homogenates when assayed spectrophotometrically. These results suggest that the antifertility effects of sodium aurothiomalate may be due to the inhibition of several sperm enzymes including both hyaluronidase and esterase. These histochemical assays may be useful for in-vivo detection of chemicals that affect male fertility.
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PMID:Histochemical evaluation of sodium aurothiomalate inhibition of mouse sperm enzymes. 642 May 52

Chondroitin 4-sulfate and chondroitin 6-sulfate were incubated with testicular hyaluronidase in the presence of excess beta-glucuronidase. The beta-glucuronidase caused rapid removal of the nonreducing terminal beta-D-glucuronosyl residues from the oligosaccharides formed by the action of the hyaluronidase, destroying the oligosaccharide acceptors required for the transglycosylation activity of hyaluronidase and releasing free D-glucuronic acid at a rate that was equal to the rate of the hyaluronidase-catalyzed hydrolysis. When hyaluronidase was assayed at 37 degrees C in the presence of 0.05 M NaCl, 0.05 M Na2SO4, and 0.1 M sodium acetate at pH 5, chondroitin 4-sulfate was hydrolyzed at 1.5 times the rate found for chondroitin 6-sulfate. When hyaluronidase was assayed at 45 degrees C in 0.06 M sodium acetate at pH 6, chondroitin 4-sulfate was hydrolyzed at 8 times the rate observed for chondroitin 6-sulfate. Under the pH5 conditions, the chondroitin 4-sulfate was converted to a mixture of tri- and pentasaccharides, while the chondroitin 6-sulfate was converted primarily to a mixture of penta- and heptasaccharides, with only a small amount of trisaccharide. Under the pH 6 conditions, the chondroitin 4-sulfate was converted to a mixture of penta- and heptasaccharides, with only a small amount of trisaccharide, but the products from chondroitin 6-sulfate were a mixture of oligosaccharides ranging in degree of polymerization from 7 to 25 monosaccharides per oligosaccharide. End-group analyses of the products formed at pH 6 showed that both substrates were cleaved preferentially at the glycosidic bonds of the 4-sulfated disaccharides.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Selective hydrolysis of chondroitin sulfates by hyaluronidase. 642 15

A procedure for the isolation of myocytes from adult rat hearts is described. It is based on successive treatments with Ca2+-free medium, disaggregating enzymes (collagenase and hyaluronidase) and mechanical agitation. Several recent isolation methods were compared and their best features were combined, together with some original modifications. A good yield of high purity myocytes with excellent morphological and functional integrity was obtained. The cells are tolerant to physiological concentrations of Ca2+. Cellular levels of ATP, Na+, and K+ are close to those in intact hearts and glucose oxidation rates and succinate exclusion are also close to normal. These characteristics are maintained for periods over 1 h.
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PMID:Isolation of Ca2+-tolerant myocytes from adult rat heart. 642 25

In this study, methods were developed for the in vitro evaluation of the surgical performance characteristics of viscoelastic fluids, such as sodium hyaluronate (Healon). Sodium hyaluronate exhibited superior surgical performance to chondroitin-6-sulfate. The superior performance of sodium hyaluronate resulted in part from its high viscosity, which is 20 times greater than that of chondroitin-6-sulfate at shear rates on the order of 10 s-1. The gel-like character of sodium hyaluronate as evidenced by the creep flow behavior, was greater than that of chondroitin-6-sulfate and was important for maintaining depth in the anterior chamber. It was shown that a threshold of 80 poise for the shear viscosity (at approximately 10 s-1 was needed for useful performance in surgery. It was also shown that 0.42 USP units of hyaluronidase per 1.0 mg sodium hyaluronate produces a 90% decrease in the shear viscosity (at approximately 10 s-1) within approximately 2 1/2 hours. Use of sodium hyaluronate in conjunction with hyaluronidase would allow sodium hyaluronate to remain highly viscous during surgery, but would gradually become less viscous to facilitate aqueous outflow after surgery.
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PMID:Shear flow characteristics of sodium hyaluronate. Relationship to performance in anterior segment surgery. 643 Feb 59

Hyaluronidase has been purified from the venom of the honey bee, Apis mellifera. The purification proved remarkably difficult, requiring a large number of chromatographic steps culminating in the removal of traces of phospholipase A2 with an affinity purified rabbit anti-phospholipase A2 immunosorbent column. The purified enzyme showed a 1143-fold increase in specific activity and was homogeneous. Electrophoresis in polyacrylamide gels (12%) containing sodium dodecyl sulphate (pH 8.9) or urea (pH 2.8) and electrofocusing in polyacrylamide (5%) gave a single band. The final product contained less than 0.1% phospholipase A2 and less than 1.5% acid phosphatase and gave a single line of precipitation against rabbit anti-hyaluronidase but was not precipitated by rabbit anti-phospholipase A2. Previous reports of instability were not confirmed, and we found the enzyme to be highly stable over a wide range of temperature and pH, and to denaturing agents. Purified hyaluronidase was found to be 'sticky' when highly pure and at low concentration, and adhered strongly to Sephadex G-75. The relative molecular mass was estimated at 35 000-37 000 by gel filtration, and at 41 000 by sodium dodecyl sulphate/polyacrylamide gel electrophoresis. A value of 50 000 was obtained by ultracentrifugation assuming a partial specific volume of 0.73 cm3/g. Hyaluronidase was found to be a minor allergen in bee venom allergic patients.
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PMID:The purification and characterisation of hyaluronidase from the venom of the honey bee, Apis mellifera. 669 11

An acidic glycoconjugate containing mannose, galactose and phosphate in approximately equimolar amounts was extracted from Leishmania donovani promastigotes and partially characterized. The glycoconjugate could be metabolically labeled with either [3H]mannose or [3H]galactose and was extractable from a delipidated residue fraction with water/ethanol/diethyl ether/pyridine/concentrated NH4OH (15:15:5:1:0.017) at 25 degrees C. The radioactively labeled glycoconjugate was found to possess the following characteristics: 1) comprised 45-60% of the total [3H]mannose label incorporated into macromolecules; 2) was soluble in alkaline solvents and 0.5% Triton X-100; 3) migrated as a broad band upon electrophoresis on sodium dodecyl sulfate-polyacrylamide gels with an approximate molecular weight of 15,000-30,000; 4) bound to DE52 cellulose and was eluted with a salt gradient of 0-0.1 M NaCl; 5) was insensitive to Pronase, hyaluronidase, chondroitinase, endo-beta-N-acetylglucosaminidase H, and endo-beta-galactosidase; and 6) possessed hydrophobic properties. An unusual feature of the glycoconjugate was its lability to mild acid hydrolysis (0.02 N HCl, 15 min, 60 degrees C). As determined by alkaline phosphatase and glycosidase digestion and paper chromatographic analysis, the major fragment generated by mild acid hydrolysis was found to be a phosphorylated galactosyl-beta-mannose disaccharide. All of these characteristics suggest that the glycoconjugate may be a polysaccharide and, possibly, may be important in parasite-host cell interactions.
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PMID:Expression of an unusual acidic glycoconjugate in Leishmania donovani. 670 85

The behavior of sodium hyaluronate injected into the anterior chamber of rabbits was investigated using a 1% (w/v) solution of sodium hyaluronate having a molecular weight of 800K. Although the aqueous humor contained a considerable amount of reduced ascorbic acid, the molecular weight of sodium hyaluronate injected into the anterior chamber did not change. This was due to existence of a protecting factor for degradation of sodium hyaluronate in a low molecular weight fraction of the aqueous humor. The injected sodium hyaluronate was found to aggregate with proteins in the aqueous humor within 2 hrs. However, this aggregation did not affect the degradation of sodium hyaluronate with ascorbic acid. The hyaluronic acid content in the iris-ciliary body increased about three times as much as the normal level 2 hrs after the sodium hyaluronate injection. This result suggests that the injected sodium hyaluronate is not only eliminated through the angular aqueous plexus but also through the iris-ciliary body, followed by digestion with hyaluronidase in those tissues.
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PMID:Biochemical studies on the use of sodium hyaluronate in the anterior eye segment. II. The molecular behavior of sodium hyaluronate injected into anterior chamber of rabbits. 671 59

The 1H-n.m.r. spectra of solutions in [2H6]dimethyl sulphoxide of the sodium salts of tetra-, hexa- and octa-saccharides prepared from hyaluronate by testicular-hyaluronidase digestion were examined at 300 and 500 MHz. The signals from hydroxy groups at positions 2 and 3 in the glucuronic acid moiety were assigned. Their chemical shifts and associated temperature-dependencies, as well as their coupling constants, depended on whether or not the uronic acid was at the non-reducing end. Deviations from the 'normal' pattern of hydroxy-group proton n.m.r. behaviour were attributable to participation in hydrogen bonds, either to the acetamido carbonyl oxygen atom or the pyranose ring oxygen atom of neighbouring N-acetylhexosamine moieties. A secondary structure, containing four different hydrogen bonds per trisaccharide unit of glucuronsyl-hexosaminyl-glucuronic acid, was demonstrated. This is the first complete and detailed secondary structure to be established for hyaluronate in any solvent. Hyaluronate is compared with chondroitin sulphate, dermatan sulphate, heparan sulphate and keratan sulphate in their potential to form secondary structures with features in common. The significance of the details of the structure to its overall stability, and the probability of their persistence into aqueous environments, are discussed. The presence of all or most of the secondary structure in glycosaminoglycuronans is correlated with a space-filling function in the tissue, and with a high carbohydrate content in the parent proteoglycan in the case of the chondroitin sulphates.
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PMID:Secondary structure of hyaluronate in solution. A 1H-n.m.r. investigation at 300 and 500 MHz in [2H6]dimethyl sulphoxide solution. 674 60


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