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 was obtained from filtrates of heat-killed cultures of Streptococcus pyogenes group A, strain K56, by simple ethanol precipitation and treatment with an adsorbent. The hyaluronic acid is pure as judged from chemical and sedimentation analyses. Particles of streptococcal bacteriophage 12/12 were isolated from phage-lysed group A streptococci by polyethylene glycol precipitation and isopyenic centrifugation. Electron micrographs of negatively stained preparations showed a typical Bradley group B virus with a long, flexible, cross-striated tail and a knob- or star-like structure at the distal tip of the tail. The hyaluronic acid is depolymerized upon incubation with the phage 12/12 virions. After extensive digestion, a mixture of at least four oligosaccharides is formed, the two smallest of which are a tetra- and octasaccharide terminating in reducing N-acetyl-D-glucosamine. The tetrasaccharide shows an absorption maximum at 231.5 nm with a molar extinction coefficient epsilon = 4820 litres X mole-1 X cm-1, and it is therefore concluded that the bacteriophage-borne hyaluronidase catalyses a beta-elimination. Accordingly it is classified as a hyaluronate lyase (EC 4.2.99.1).
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PMID:Streptococcal bacteriophage 12/12-borne hyaluronidase and its characterization as a lyase (EC 4.2.99.1) by means of streptococcal hyaluronic acid and purified bacteriophage suspensions. 79 93

The capacity of non-pepsinyzed type VI collagen to bind to hyaluronan was investigated. Type VI collagen was extracted from bovine meniscal cartilage with 6 M GuHCl and purified by extraction of PEG precipitates and dissociative Sephacryl S-500 HR chromatography. Type VI collagen, detected with a monoclonal antibody, bound in 0.5 M NaCl to hyaluronan-coated micro-wells, the degree of binding being higher at 37 degrees C than 23 degrees C and 4 degrees C. Incubation of type VI collagen in competitive inhibition assays with testicular hyaluronidase digests of hyaluronan in liquid phase, reduced binding of the protein to hyaluronan-coated microwells to background levels. Thus, non-pepsinyzed type VI collagen binds to hyaluronan in vitro.
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PMID:Interaction of intact type VI collagen with hyaluronan. 175 55

Seventy five prostatic specimens from cancer, BPH and normal controls were studied by light microscopic histochemical methods for the demonstration of complex carbohydrates and some proteins: 1) alcian blue (AB) (pH 1.0), 2) alcian blue (AB) (pH 2.5), 3) Periodic Acid-Schiff (PAS), 4) peroxidase labelled-Ricinus communis agglutinin-diaminobenzidine (PO-RCA-DAB), 5) Concanavalin A-peroxidase-diaminobenzidine (ConA-PO-DAB), 6) ConA-PO-DAB-periodic acid-m-aminophenol Fast black salt K (ConA-PO-DAB-PA-AP-FBK). For identifying individual acidic and neutral carbohydrates, following procedures of enzyme digestion were performed upon some tissue sections prior to the above histochemical staining: a) sialidase (prior to staining with AB at pH 2.5), b) streptomyces hyaluronidase (prior to staining with AB at pH 2.5), c) testicular hyaluronidase (prior to staining with AB at pH 1.0 or pH 2.5), d) chondroitinase ABC (prior to staining with AB at pH 1.0 or pH 2.5), e) chondroitinase AC (prior to staining with AB at pH 1.0 or pH 2.5), f) alpha-amylase (prior to staining with PAS). In addition, the tissue specimens from prostatic cancer were stained immunohistochemically for demonstration of prostatic acid phosphatase (PAP) and the serum PAP levels were also measured by radioimmunoassay. The histochemical differences in the prostatic tissue among normal control, BPH and cancer as follows. In the tissue of prostatic cancer, chondroitin sulfate A, C and hyaluronic acid were present in the interstitium. Chondroitin sulfate, hyaluronic acid and sialic acid were present in the cytoplasm of cancer cells. In the tissue of BPH chondroitin sulfate B and hyaluronic acid was present in the interstitium and hyaluronic acid was present in the cytoplasm of epitherial cells. In the epithelial basement membrane of the tissue from BPH, chondroitin B and hyaluronic acid were present. 1,2-Glycol groups of neutral complex carbohydrates in the interstitium of prostatic cancer were shown to exist in smaller amounts than in that of BPH. In the cytoplasm of cancer cells the intensity of both PO-RCA-DAB and ConA-PO-DAB staining could be divided into three groups: strong, moderate and weak. In the prostatic cancer there was a good correlation between the intensity of PO-RCA-DAB staining and tumor grade, and intensity of ConA-PO-DAB staining was correlated well with serum PAP level. The cytoplasm of cancer cells showed a positive reaction to PAP immunostaining and no appreciable difference was observed according to tumor grade.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:[The histochemistry of complex carbohydrates in the prostatic tumor]. 258 29

An investigation was made of the inter-relationships and characteristics of various hyaluronidase forms isolated from ram spermatozoa. They were shown to be members of an oligomeric series, apparently formed by intermolecular disulphide cross-linking. Two monomer species were detected, alpha (Mr 89,600) and beta (Mr 81,200). Although the alpha species predominated, the two were evenly distributed throughout the oligomer population, and they shared antigenic determinants; the beta species did not arise from the alpha species as a result of catabolism following cell disruption. The oligomeric series was of the form [Hyal]n, where n = 1, 2, 4, 5, 6, 7 etc.; no trimer was detectable. Though essentially cationic, part of the hyaluronidase population also had anionic characteristics, probably due to oxidation of free thiol groups. In the anionic subpopulation tetramers and higher oligomers predominated, whereas the non-anionic subpopulation was composed of monomers, dimers and tetramers. The pH optimum of the monomer was 4.3 in 0.2 M-NaCl/0.1 M-sodium citrate, whereas that of the anionic oligomers was 4.9. Both serum albumin and polylysine stimulated enzyme activity at pH 4.0 in the absence of NaCl; polylysine was particularly effective. NaCl diminished the stimulatory effects, and essentially suppressed them above the pH optimum. The specific activities of different oligomer populations were the same as that of the monomer, and conversion of oligomers into monomer by reduction had likewise no effect upon the specific activity. Low concentrations of poly(vinyl alcohol), poly(ethylene glycol) or polyvinylpyrrolidone stabilized soluble hyaluronidase activity by preventing the enzyme's binding to surfaces; solutions of anionic oligomers were further stabilized by NaCl. Enzyme preparations were stable for several months frozen in the presence of poly(vinyl alcohol) and salt.
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PMID:Preliminary characterization of the multiple forms of ram sperm hyaluronidase. 342 27

The binding of radiolabeled GnRH and GnRH agonist (GnRHA) was studied in homogenates of human luteal tissue using a polyethylene glycol precipitation technique. GnRHA binding to human luteal homogenates was dependent on pH, was inhibited by a number of divalent metal ions, and was of moderately high affinity (Ka = 3 X 10(7) M-1). Binding of both radiolabeled GnRH and GnRHA increased linearly with increasing homogenate concentration, and binding of either tracer was parallel with different corpus luteum (CL) homogenates. Moreover, similar concentrations of unlabeled GnRH or GnRHA blocked the binding of either tracer, indicating that both hormones bound to a common site. The rate of dissociation of bound ligand was very low at 0 C, but was extremely rapid at physiological temperatures (t1/2 = 2.5-3.5 min). Human luteal GnRHA-binding sites were partially solubilized by treatment with Triton X-100 and were sensitive to trypsin and pronase, but not hyaluronidase. GnRHA binding to homogenates of human CL obtained at each stage of the luteal phase varied markedly, with levels ranging from less than 20 to greater than 1600 pg/mg DNA for CL from the (midluteal) stage of the menstrual cycle. This variability could not be accounted for by assay irreproducibility, loss of binding activity during storage, or occupancy of binding sites by endogenous ligand. These observations may help to explain negative reports from other groups, which demonstrated little or no specific binding of GnRH to human luteal tissue and no effect of GnRH on steroidogenesis using dispersed human luteal cells in vitro. We conclude that human luteal homogenates possess specific, moderately high affinity binding sites for GnRH and its agonist analogs.
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PMID:Specific binding of gonadotrophin-releasing hormone and an agonist to human corpus luteum homogenates: characterization, properties, and luteal phase levels. 393 May 50

Oxfendazole (methyl 5-(phenylsulfinyl)-2-benzimidazole-carbamate) is a broad spectrum anthelmintic agent designed for use in food-producing animals. A simple radioimmunoassay (RIA) for determination of oxfendazole in plasma was modified for determining oxfendazole in sheep fat. Fat tissue was enzymatically hydrolyzed to an oily residue with collagenase-hyaluronidase, and oxfendazole was then extracted into an acidified aqueous phase. An aliquot of this phase was used directly for RIA. Bound radioactivity was separated from free by using polyethylene glycol-bovine gamma globulin because oils and other components in the aqueous aliquot preclude the use of charcoal for the separation. The lower limit of sensitivity of the assay is 0.003 ppm. Accuracy experiments carried out in the range 0.01-0.5 ppm gave a regression line of y (ng/g) = 0.91 x (ng/g) + 2.89, with r = 0.99. Fat tissue derived from sheep given an oral dose of 6.0 mg/kg was analyzed by this method and by a high pressure liquid chromatographic (HPLC) method. Values obtained by the 2 methods agreed well.
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PMID:Radioimmunoassay of oxfendazole in sheep fat. 709 45

To study the contribution of tissue components to the mechanical properties of veins, pressure-volume relationships were obtained with the cylindrical segments of isolated dog external jugular veins at several levels of longitudinal extension. At each length, the transmural pressure of the segment was raised up to 20 cmH2O and then reduced to 0 cmH2O by increasing and decreasing the intraluminal volume at a constant rate. The longitudinal extension of the venous segments caused a significant reduction in the incremental volume elasticity within the pressure range of 0-2 cmH2O (E0-2) as well as a significant increase of the incremental volume elasticity within 10-20 cmH2O (E10-20). The pressure-volume relationships of venous segments were also constructed in the same way after treatment with 1 mg/ml collagenase for 30 min, 0.1 mg/ml elastase for 5 min, or 1 mg/ml hyaluronidase for 60 min. Treatment with collagenase or elastase produced a significant increase of the E0-2. The treatment, however, caused no effect on E10-20. Treatment with hyaluronidase induced no effect on these mechanical parameters but produced a significant attenuation of the extension-induced decrease in E0-2. Activation of the venous smooth muscles induced by norepinephrine (10(-4) M) or high-potassium Krebs solution caused a significant decrease of E0-2 as well as a significant increase of E10-20. A complete relaxation of the smooth muscles elicited by Ca(2+)-free Krebs solution containing ethylene glycol-bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid (2 mM) caused an increase of E0-2. Mechanical rubbing of the endothelium caused no significant effect on E0-2 and E10-20.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Effects of collagenase, elastase, and hyaluronidase on mechanical properties of isolated dog jugular veins. 834 43

A new hyaluronic acid (HA)-based hydrogel film was prepared and evaluated for use in drug delivery. This biocompatible material crosslinks and gels in minutes, and the dried film swells and rehydrates to a flexible hydrogel in seconds. HA was first converted to the adipic dihydrazide derivative and then crosslinked with the macromolecular homobifunctional reagent poly(ethylene glycol)-propiondialdehyde to give a polymer network. After gelation, a solvent casting method was used to obtain a HA hydrogel film. The dried film swelled sevenfold in volume in buffer, reaching equilibrium in less than 100 s. Scanning electron microscopy (SEM) of the hydrogel films showed a condensed and featureless structure before swelling, but a porous microstructure when hydrated. The thermal behavior of the hydrogel films was characterized by differential scanning calorimetry. The enzymatic degradation of the HA hydrogel films by hyaluronidase was studied using both SEM and a spectrophotometric assay. Drug release from the hydrogel film was evaluated in vitro using selected anti-bacterial and anti-inflammatory drugs. This novel biomaterial can be employed for controlled release of therapeutic agents at wound sites.
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PMID:Cross-linked hyaluronic acid hydrogel films: new biomaterials for drug delivery. 1101 55

The objective of this work was to develop an effective vitrification technique for cryopreserving oocytes in sheep ovarian tissues. Ovaries were surgically recovered from 15 pubertal ewes and the ovarian cortex was cut into sections. Ovarian tissues were placed in equilibration medium consisting of 4% (v/v) ethylene glycol (EG) and 20% (v/v) FBS in TCM-199 on ice for 30 min and transferred to vitrification solution (35% EG, 5% polyvinylpyrrolidone, 0.4M trehalose and 20% FBS in TCM-199) for 5 min. Ovarian tissues were vitrified by dropping the tissue on the surface of a steel cube cooled by liquid nitrogen. Cumulus-enclosed oocyte complexes (COC) were also collected and vitrified following the procedure used for ovarian tissues. After 2-3 weeks of storage in liquid nitrogen, ovarian tissues and COC were thawed at 37 degrees C in 0.3M trehalose and COC in ovarian tissues were mechanically and enzymatically isolated. Vitrified COC and freshly collected COC were washed twice in maturation medium (TCM-199 supplemented with 0.255 mM pyruvate and 10% heat-treated estrus cow serum) and cultured in 50 microl drops of maturation medium under paraffin oil for 23-25h at 39 degrees C in a humidified atmosphere of 5% CO(2) in air. After culture, cumulus cells were removed by hyaluronidase treatment and vortexing and oocytes were fixed and stained. No significant differences were observed between vitrified oocytes, oocytes recovered from vitrified ovarian tissues and non-vitrified control oocytes in the percentage of oocytes with acceptable staining per total number of oocytes fixed or with visible chromatin per total number of oocytes with acceptable staining. However, fewer (P<0.05) oocytes obtained from vitrified ovarian tissues (70%) reached metaphase II compared to vitrified oocytes (88%) and non-vitrified control oocytes (90%). In contrast, when oocytes with at least 3-5 layers of cumulus cells were considered from each of the three groups, no differences (P>0.05) were observed due to treatment in the percentages of oocytes developing to metaphase II. These results demonstrate that sheep oocytes can be successfully cryopreserved by vitrification of ovarian tissues and exhibit in vitro maturation rates similar to that of vitrified and non-vitrified oocytes.
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PMID:Survival of oocytes recovered from vitrified sheep ovarian tissues. 1198 74

Hyaluronic acid (HA) was derivatized with methacrylic esters used for the preparation of hydrogels via photopolymerization. Poly(ethylene glycol) diacrylate (PEG-DA) with a molecular weight of 570 was also used as a comacromonomer to improve elastic modulus and swelling behavior. The hydrogels were readily degraded by hyaluronidase and their mechanical properties could be modulated by HA molecular weight and concentration of PEG-DA. The incorporation of RGD peptides allowed modulation of the HA properties from cell non-adhesive to adhesive. Human dermal fibroblasts were cultured on the RGD, RDG, and non-functionalized HA hydrogels for up to 7d, showing adhesion and proliferation only with incorporated RGD.
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PMID:Photopolymerized hyaluronic acid-based hydrogels and interpenetrating networks. 1250 9


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