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)

Hyaluronidase release was used as an index of acrosomal membrane damage during cold shock of epididymal boar sperm and ejaculated sperm from intact and vesiculectomized boars. Sperm were also incubated with seminal plasma from intact and vasectomized boars to examine the contributions of male accessory gland secretions. Acrosomal membranes of epididymal sperm were more resistant to cold shock than those of ejaculated sperm. Only 36% of the hyaluronidase released by ejaculated sperm was released by the epididymal sperm in spite of similar hyaluronidase content of the sperm. Preincubation of epididymal sperm in seminal plasma from both intact and vasectomized boars increased resistance to cold shock by 60 to 80%. Initial dilution of epididymal sperm with seminal plasma, rather than Ringer-fructose buffer, was associated with low progressive motility and with retention of cytoplasmic droplets. In contrast, acrosomal membranes of ejaculated sperm from intact and vesiculectomized boars exhibited similar sensitivity to cold shock, releasing hyaluronidase capable of forming .20 and .19 mumol N-acetylglucosamine from hyaluronic acid/10(8) sperm in 8 min. Moreover, seminal plasma from vasectomized boars had no effect on acrosomal sensitivity to cold shock of ejaculated sperm from vesiculectomized boars.
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PMID:Effect of male accessory gland secretions on sensitivity of porcine sperm acrosomes to cold shock, initiation of motility and loss of cytoplasmic droplets. 400 68

The murine monoclonal antibody (MAb) designated DF3 has defined a high m.w. antigen detectable in human breast carcinomas and in human milk. DF3 antigen is detectable on apical borders of secretory mammary epithelial cells and in the cytosol of less differentiated malignant cells. DF3 antigen expression has been shown to correlate with the degree of human breast tumor differentiation, and the detection of a cross-reactive species in human milk has suggested that DF3 antigen might be useful as a biochemical marker of differentiated mammary epithelial cells. To further characterize DF3 antigen, we have developed an approach to purify the cross-reactive species by using gel filtration and antibody affinity chromatography. The affinity column-purified DF3 antigen was absorbed by wheat germ agglutinin and peanut agglutinin, but not by concanavalin A or lentil lectin. In contrast, wheat germ agglutinin inhibited MAb DF3 reactivity with the purified antigen, whereas there was little, if any, inhibition when using peanut agglutinin. These findings are thus consistent with the involvement of terminal N-acetyl-D-neuraminic acid and/or N-acetylglucosamine residues in the antigenic site. DF3 antigenicity was also sensitive to neuraminidase, but not chondroitinase ABC, chondroitinase AC, chondroitin-4-sulfatase, or hyaluronidase. Furthermore, DF3 antigen was sensitive to Pronase, subtilisin BPN', and alpha-chymotrypsin. The presence of O-glycosidic linkages between carbohydrate and protein in the DF3 antigenic site was further supported by the presence of NaBH4-sensitive sites. Together, these results suggest that sialyl oligosaccharides present on a peptide backbone are required for maintaining DF3 antigenicity. Similar findings have been demonstrated for DF3 antigen purified from both human milk and breast cancer effusions. However, the DF3 antigen in human milk consisted of a single high m.w. species, whereas the tumor-associated antigen consisted of two distinct glycoproteins with m.w. of 330,000 and 450,000. These findings may be relevant to the recent demonstration that distinct high m.w. DF3 antigens are elevated in the circulation of patients with breast carcinoma.
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PMID:Purification and characterization of a high molecular weight glycoprotein detectable in human milk and breast carcinomas. 404 99

1. Methods for the purification of dog submandibular-gland hyaluronidase from sedimentable and non-sedimentable portions of a homogenate and from the whole homogenate are presented. The method consists of three main steps: removal of mucin by acid precipitation or gel filtration on Sephadex G-200, ammonium sulphate precipitation and CM-cellulose chromatography. By this method specific activities of up to 1.28 and 0.78mumoles of N-acetylglucosamine/min./mg. of protein were obtained for the purified freeze-dried non-sedimentable hyaluronidase and for the sedimentable hyaluronidase respectively. 2. A comparison of some of the properties of the non-sedimentable and the sedimentable hyaluronidase preparation indicated that there was little difference between the two and that they both resembled lysosomal hyaluronidase from rat liver.
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PMID:Canine submandibular-gland hyaluronidase. Purification and properties. 572 88

Hyaluronidase (hyaluronate 4-glycanohydrolase, EC 3.2.1.35) was purified from mouse testes by ion-exchange chromatography, Sephadex G-200 filtration and Con A-agarose affinity chromatography. The final preparation had 94-fold purity and 12.2 units spec. act. of the enzyme (unit of specific activity = mumol N-acetylglucosamine released/h per mg protein at 37 degrees C and pH 4.5). Hyaluronidase is relatively heat stable and loses 10-20% of its activity at 50-55 degrees C for 10 min. Ea for eat denaturation of enzyme is 42-45 kcal between 45 an 63 degrees C. The Michaelis constant of mouse testicular hyaluronidase is 1.1 mg/ml hyaluronic acid. Antibodies to the purified enzyme were produced in rabbits and showed a single precipitin line by Ouchterlony gel diffusion. Antiserum to hyaluronidase inhibited enzyme activity by 25%. Immunologically, mouse testicular hyaluronidase is species specific. Tissue extracts of mouse vital organs, except testes and epididymis did not react with the antisera, though nonspecific precipitation occurred between intestinal extracts and anti-hyaluronidase serum. Hyaluronidase was localized in testis sections by indirect immunofluorescence. A specific dark green fluorescence was localized on cell boundaries extending from spermatogonia to spermatids and appeared on the sperm acrosome. Cytoplasm of spermatogonia and spermatocytes showed light green fluorescence, whereas interstitial tissue was devoid of fluorescence.
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PMID:Isolation, properties, immunological specificity and localization of mouse testicular hyaluronidase. 616 67

Experiments with immobilized concanavalin A strongly suggest a glycoprotein nature of three honey-bee venom enzymes, phospholipase A2, hyaluronidase and acid phosphatase. The electrophoretically and chromatographically detectable heterogeneity of phospholipase A2 results from absence of carbohydrate in a subfraction. Mannose, fucose and N-acetylglucosamine, but not galactose nor N-acetylgalactosamine, are present in the con A-binding fraction of bee venom. It is therefore concluded that only N-glycosidically linked carbohydrate occurs in bee venom glycoproteins.
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PMID:The glycoprotein nature of phospholipase A2, hyaluronidase and acid phosphatase from honey-bee venom. 665 11

Teratocarcinoma cells (F9) were induced to differentiate by retinoic acid and then labelled with [3H]-glucosamine and [35S]-sulphate. Proteoglycans were then isolated from the plasma membranes and the culture medium by mild, dissociative, non-shear-dependent techniques. The undifferentiated cells were devoid of hyaluronic acid and contained negligible quantities of heparan sulphate, dermatan sulphate and chondroitin sulphate. Upon differentiation, the cells synthesized large amounts of hyaluronic acid and there was a threefold increase in the amount of membrane-bound sulphated proteoglycans. The differentiated cells also synthesized a proteoglycan (PGM-2) which was shed completely into the medium. It consisted of a large protein core with covalently linked sugar chains which were sulphated and had an approximate molecular weight of 12000. These sugar chains consisted of glucosamine and galactose in a molar ratio of 1:1 and contained a small quantity of mannose. Upon differentiation of the cells the amount of this molecule increased by threefold. This molecule was distinct from other proteoglycans since it was resistant to degradation by heparanase, chondroitinases, hyaluronidase and neuraminidase, but could be degraded by keratanase. Structurally it was very similar to keratan sulphate, consisting of alternating residues of (-Gal-GlcNAc-) in chains of approximately 20 such disaccharide units.
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PMID:Changes in proteoglycan composition of F9 teratocarcinoma cells upon differentiation. 666 12

Human vascular endothelial cells synthesize lactosaminoglycan-type glycoproteins which are found both associated with cells and secreted into the culture medium. Pronase-derived glycopeptides prepared from [3H]glucosamine-labeled glycoproteins were found to contain about 10% of the labeled products as a large size (Mr greater than 5000) 3H-labeled glycopeptide. Digestion of these 3H-labeled glycopeptides with endo-beta-galactosidase resulted in the release of smaller size saccharides, which were characterized as having the structure sialic acid----Gal----GlcNAc----Gal. Treatment of [3H]glucosamine-labeled cells with melittin caused 3H-labeled glycoconjugates to be released from the cells. Separation of released glycoproteins from proteoglycans by DEAE-cellulose chromatography indicated that melittin had released 25% of the total 3H-labeled glycoproteins from the cell and 3% of the 3H-labeled proteoglycans. The 3H-labeled glycoproteins were digested with Pronase and the resulting 3H-labeled glycopeptides were fractionated on Sephadex G-50. The large size fraction (Mr greater than 5000) now comprised about 30% of these released 3H-labeled glycopeptides. These high molecular weight 3H-labeled glycopeptides were degraded with endo-beta-galactosidase but not with testicular hyaluronidase. Analysis of the released 3H-labeled glycoproteins indicated a preferential release of glycoproteins of 70-90 kDa enriched in lactosaminoglycan-type oligosaccharides.
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PMID:Synthesis of lactosaminoglycan-containing glycoproteins by vascular endothelial cells. 670 15

The hybrid cell B6 line, which synthesizes large amounts of hyaluronate as the predominant glycosaminoglycan, was grown in the presence of [3H]glucosamine. The [3H]hyaluronate has a high molecular weight and was excluded by Sephacryl S-1000. After disruption of the cells the [3H]hyaluronate could further be elongated by incubation with UDP-GlcNAc and UDP-[14C]GlcA, yielding a hybrid molecule of hyaluronate labelled with [3H]GlcNAc and [14C]GlcA. Treatment of the cells with hyaluronidase before disruption eliminated the large [3H]hyaluronate and elongation of nascent chains in vitro commenced from low-molecular-weight chains. Thus nascent hyaluronate chains were degraded extracellularly by hyaluronidase and were therefore synthesized at the inner side of plasma membranes and extruded to the cell surface.
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PMID:Hyaluronate is synthesized at plasma membranes. 674 90

Hyaluronidase from the venom of the honeybee (Apis mellifera) has been purified by gelpermeation and cation exchange chromatography. Its asparagine-linked carbohydrate chains were released from tryptic glycopeptides with N-glycosidase A and reductively aminated with 2-aminopyridine. Separation of the fluorescent derivatives by size-fractionation and reversed-phase HPLC afforded eighteen fractions which were analysed by two-dimensional HPLC mapping combined with exoglycosidase digestions. The bulk of the N-linked glycans of hyaluronidase consisted of small oligosaccharides (Man1-3GlcNAc2), most of which were either alpha 1,3-monofucosylated or alpha 1,3-(alpha 1,6-)difucosylated at the innermost GlcNAc residue. High-mannose type structures constituted the minor fractions, together making up about 5% of the oligosaccharide pool from hyaluronidase. Four fractions, making up 8% of the N-linked glycans, contained the terminal trisaccharide GalNAc beta 1-4[Fuc alpha 1-3]GlcNAc beta 1- in beta 1,2-linkage to the core alpha 1,3-mannosyl residue. No evidence for the presence of O-glycans or sialic acids could be found.
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PMID:The asparagine-linked carbohydrate of honeybee venom hyaluronidase. 779 17

Streptococcus intermedius strain UNS 35, a brain abscess isolate, produced extracellular hyaluronidase when grown in brain heart infusion broth. Chemical assays with this enzyme indicated that hyaluronate depolymerisation resulted in the formation of carbohydrate moieties with N-acetylglucosamine at the reducing terminal and containing an unsaturated carbon-carbon double bond. The nature of the products of this hyaluronidase were investigated further by high-field (400 MHz) proton (1H) NMR spectroscopy. Treatment of hyaluronate with the enzyme resulted in a series of new, sharp resonances in spectra (acetamido methyl group singlets located at 2.03 and 2.07 ppm, sugar ring proton multiplets in the 3.5-4.2 ppm chemical shift range, and doublets at 5.16 and 5.87 ppm) characteristic of low-M(r) oligosaccharide species, predominantly those containing glucuronosyl residues with delta 4,5-carbon-carbon double bonds. Comparison of spectra acquired from hyaluronidase-treated samples with that of an authentic sample of 4-deoxy-L-threo-hex-4-enopyranosyluronic-acid-N-acetylglucosamine (delta UA GlcNAc) indicated that this disaccharide was a major product arising from the actions of this enzyme. When used in minimal media, hyaluronate supported growth of S. intermedius, with lactate as the major metabolic end-product.
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PMID:Degradation of hyaluronate by Streptococcus intermedius strain UNS 35. 796 19


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