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

---

Query: EC:3.2.1.36 (hyaluronidase)
4,606 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

When cells dissociated from the neonatal rat brains are plated on a poly-lysine-coated surface in a serum-free medium, they display a strange morphology: a dark and extended cell body. Preincubation of the surface with fetal bovine serum was found to inhibit the appearance of this strange contraction of the basal cell sheets in a dose-dependent manner. This finding indicated the presence of a factor(s) in the serum, which might be an appropriate substratum for prolonged survival of brain neurons. In the current study, this factor was highly purified through DEAE ion-exchange chromatography followed by gel filtration. The factor was eluted from a Superose column at fractions corresponding to a molecular weight greater than 1000 kDa. By SDS-PAGE analysis, these fractions were found to contain a major band (>/=1000 kDa) positive for alcian blue and few minor bands faintly stainable with Coomassie blue. The activity of the purified sample, inducing the morphological change in cells, was diminished by incubation with chondroitinase ABC. Neither heparitinase II, hyaluronidase, nor trypsin modified the activity. An authentic chondroitin sulfate (type B) mimicked the serum action on the morphology of brain cells in early stages of culture. Taking these findings together, it is suggested that the factor in serum beneficial for the attachment of brain cells is composed of a chondroitin sulfate with a Mr greater than 1000 kDa. Cortical cells dissociated from the neonatal rat brain attached well to the purified factor-coated surface and displayed a healthy morphology: an optically-reflective cell body with thick neurites for at least 3 days in the absence of serum.
...
PMID:A culture substratum appropriate for brain cells is a chondroitin sulfate glycosaminoglycan in serum. 947 1

Venoms from the scorpaeniformes Synanceja trachynis and Gymnapistes marmoratus were quantitatively analyzed for enzymic activity. S. trachynis venom displayed significantly higher hyaluronidase activity than G. marmoratus venom, and G. marmoratus venom displayed significantly higher levels of esterase, acid phosphatase, alkaline phosphatase and phosphodiesterase activity. No detectable quantities of phospholipase A2 activity were found in G. marmoratus venom. SDS-polyacrylamide gel electrophoresis of S. trachynis venom indicated the presence of 6 protein bands (20 kDa-295 kDa). G. marmoratus venom displayed 8 protein bands (11 kDa-109 kDa).
...
PMID:Enzyme and biochemical studies of stonefish (Synanceja trachynis) and soldierfish (Gymnapistes marmoratus) venoms. 965 39

Glycoprotein showing inhibitory activity against mast cell degranulation and hyaluronidase activity was purified from the hot water extract of mint plant (Perilla frutescens Britton). The purified inhibitor gave a single band detected with Coomassie brilliant blue staining and periodic acid-Schiff staining on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis. The molecular mass was estimated to be 6.0 kDa on SDS-PAGE. The inhibitor did not become inactivated when boiled for 30 min or digested with trypsin, V8 protease, or proteinase K but was inactivated by NaIO(4) oxidation. The inhibitor prevented mast cell degranulation and hyaluronidase activity (IC(50) = 0.42 mg/mL) in a dose-dependent manner. The inhibitor also inhibited the protein kinase C activity. It is possible to purify and characterize a glycoprotein with putative pharmacological properties from mint plants.
...
PMID:Glycoprotein derived from the hot water extract of mint plant, Perilla frutescens britton. 1056 18

R.E. Hill and S.P. Mackessy. Characterization of venom (Duvernoy's secretion) from twelve species of colubrid snakes and partial sequence of four venom proteins. Toxicon XX, xx-yy, 2000. - Venomous colubrids, which include more than 700 snake species worldwide, represent a vast potential source of novel biological compounds. The present study characterized venom (Duvernoy's gland secretion) collected from twelve species of opisthoglyphous (rear-fanged) colubrid snakes, an extremely diverse assemblage of non-venomous to highly venomous snakes. Most venoms displayed proteolytic activity (casein), though activity levels varied considerably. Low phosphodiesterase activity was detected in several venoms (Amphiesma stolata, Diadophis punctatus, Heterodon nasicus kennerlyi, H. n. nasicus and Thamnophis elegans vagrans), and acetylcholinesterase was found in Boiga irregularis saliva and venom, but no venoms displayed hyaluronidase, thrombin-like or kallikrein-like activities. High phospholipase A(2) (PLA(2)) activity was found in Trimorphodon biscutatus lambda venom, and moderate levels were detected in Boiga dendrophila and D. p. regalis venoms as well as B. dendrophila and H. n. nasicus salivas. Non-reducing SDS-PAGE revealed 7-20 protein bands (3.5 to over 200 kD, depending on species) for all venoms analyzed, and electrophoretic profiles of venoms were typically quite distinct from saliva profiles. Components from A. stolata, Hydrodynastes gigas, Tantilla nigriceps and T. e. vagrans venoms showed protease activity when run on gelatin zymogram gels. N-terminal protein sequences for three 26 kD venom components of three species (H. gigas, H. torquata, T. biscutatus) and one 3.5 kD component (T. nigriceps) were also obtained, and the 3.5 kD peptide showed apparent sequence homology with human vascular endothelial growth factor; these data represent the first sequences of colubrid venom components. Protease, phosphodiesterase and PLA(2) activities are also common to elapid and viperid snake venoms, but it is apparent that numerous other (as yet undescribed) components make up the majority of colubrid venom proteins. The complex nature of venoms produced by most species surveyed, and the high levels of protease or phospholipase A(2) activity of some venoms, suggest that many colubrids could become an important source of human health concern as encounters with these snakes increase.
...
PMID:Characterization of venom (Duvernoy's secretion) from twelve species of colubrid snakes and partial sequence of four venom proteins. 1085 9

A method has been developed which allows the analysis of glycoproteins separated by SDS-PAGE. The procedure, though applicable to N-glycosylated glycoproteins of any origin, is particularly devised for glycoproteins potentially containing fucose in alpha1,3-linkage to the reducing GlcNAc as may be found in plants and invertebrates, e.g., insects and parasitic helminths. Starting with an established procedure for mass spectrometric peptide mapping, the analysis of N-glycans by matrix-assisted laser desorption/ionization mass spectrometry involved the use of peptide:N-glycosidase A, a triphasic microcolumn for sample cleanup, and a new matrix mixture consisting of 2,5-dihyhydroxybenzoic acid, 1-hydroxyisoquinoline, and arabinosazone. The method was tested on proteins with N-glycans of known structure, i.e., as horseradish peroxidase, zucchini ascorbate oxidase, soybean agglutinin, honeybee venom hyaluronidase, bovine ribonuclease B, and bovine fetuin. An electrophoretic band corresponding to 4 microg of glycoprotein was generally sufficient to allow detection of the major N-glycan species. As an additional benefit, a peptide mass map is generated which serves to identify the analyzed protein. The method was applied to glycoprotein allergens whose glycan structures were unknown. Ara h 1 and Ole e 1, major allergens from peanut and olive pollen, respectively, contained mainly xylosylated N-glycans with the composition Man(3(-4))XylGlcNAc(2) in the case of Ara h 1 and GlcNAc(1-2)Man(3)XylGlcNAc(2) in the case of Ole e 1 where also some GlcNAc(0-2)Man(3)XylFucGlcNAc(2) was found.
...
PMID:N-Glycan analysis by matrix-assisted laser desorption/ionization mass spectrometry of electrophoretically separated nonmammalian proteins: application to peanut allergen Ara h 1 and olive pollen allergen Ole e 1. 1099 64

An enzyme that degraded glycosaminoglycan hyaluronic acid was released during in vitro development of Ascaris suum L3 to L4. The enzyme did not hydrolyze glycosaminoglycan chondroitin sulfate A. One molecular form of hyaluronidase was detected, with a molecular weight estimated at 47.8 +/- 8.6 kDa by sucrose density gradient centrifugation and at 55.0 +/- 1.3 kDa by substrate SDS-PAGE zymography. Activity of the enzyme was optimal between pH 5.0 and 6.0, and was present at neutral pH. Hyaluronidase activity was not affected by 5 mM concentrations of cupric sulfate, zinc chloride, calcium chloride, manganese chloride or EDTA. In addition, NaCl had no effect on enzyme activity at concentrations of 0.2-1.0 M. The highest level of hyaluronidase was present in culture fluid collected between days 4 and 6 of in vitro culture, and this period corresponded with that of the highest rate of increase in the percentage of L4. The presence or absence of hyaluronic acid plays a key role in basic developmental processes of vertebrates and is regulated, in part, by hyaluronidases. Developmental processes occurring during the transition of A. suum L3 to L4 may likewise depend on hyaluronidase. In addition, the infection process of a number of organisms, including some nematodes, depends on hyaluronidase. A. suum may likewise utilize hyaluronidase to facilitate larval migration within the host.
...
PMID:Release of hyaluronidase during in vitro development of Ascaris suum from the third to fourth larval stage. 1157 May 51

It is generally accepted that spermatozoa become functionally mature during epididymal transit. The objective of this study was to determine whether the cellular location of equine PH-20 is modified during epididymal transit and, if so, the mechanism for such modification. Sperm were isolated from caput and cauda epididymal regions from stallions undergoing castration (n = 7) and used as whole sperm cell or subjected to nitrogen cavitation for isolation of plasma membrane proteins. Both caput and cauda sperm and sperm protein extracts were subjected to N-deglycosylation, O-deglycosylation, or trypsinization. The SDS-PAGE and Western blot analysis using a polyclonal anti-equine PH-20 IgG were performed in sperm extracts, and indirect immunofluorescence on whole sperm was also performed to determine the cellular distribution of plasma membrane PH-20 following similar treatments (deglycosylation or trypsinization). Hyaluronan substrate gel electrophoresis was performed to detect hyaluronidase activity in SDS-PAGE proteins. Western blots revealed significant differences in electrophoretic migration of PH-20 proteins from caput and cauda epididymal sperm. No effect was seen from deglycosylation treatments on the Western blot pattern; caput protein extracts exposed to trypsin showed the same band pattern as extracts from the cauda epididymis. N-deglycosylation resulted in the loss of hyaluronidase activity of sperm from both epididymal regions, whereas O-deglycosylation or trypsinization did not affect hyaluronidase activity. In caput epididymal sperm, the PH-20 protein is distributed over the entire sperm head; in cauda epididymal sperm, it is restricted to the postacrosomal region. No effect from deglycosylation on the cellular distribution of PH-20 was observed; however, treatment with trypsin changed the cellular distribution of PH-20 in caput sperm similar to that of the distribution of cauda sperm. These results suggest that PH-20 distribution during epididymal maturation is dependent on proteolytic trypsin-like mechanisms and, possibly, on complementary membrane-associated factors.
...
PMID:Posttranslational processing of PH-20 during epididymal sperm maturation in the horse. 1167 46

The purpose of this study was to examine the corneal toxicity of different preparations of intraocular hyaluronidase. SDS-PAGE analysis of bovine testicular hyaluronidase (Wydase) and chromatographically purified hyaluronidase (Sigma) was performed. These two preparations were injected into the anterior chamber of rabbits in amounts ranging from 1.5-150 IU (Wydase) and 1.5-300 IU (Sigma). A third set of rabbit eyes received Wydase vehicle alone or in combination with Sigma hyaluronidase. Treated control eyes were injected with saline. Slit lamp examination and indirect ophthalmoscopy were performed preoperatively and on postoperative days 1 and 7. Light microscopy of the corneas was performed. SDS-PAGE of Wydase revealed numerous protein impurities, while Sigma demonstrated one protein band consistent with mammalian hyaluronidase. Persistent corneal edema, severe anterior chamber fibrin, and endothelial necrosis, were seen in the majority of eyes injected with Wydase in amounts of 50 IU and greater (n = 11). Thirty percent (30%) of the eyes injected with the Sigma preparation (n = 11) had localized corneal opacity similar to 50% of eyes injected with saline (n = 2). Of the rabbit eyes injected with the Wydase vehicle (n = 19), 68% had toxic changes. Intracameral injection of Wydase is toxic to the rabbit cornea in amounts of 50 IU and greater. A chromatographically purified preparation showed only transient local toxicity. Toxicity of Wydase may be due to protein impurities and the thimerosal-containing vehicle.
...
PMID:Corneal toxicity of intraocular hyaluronidase. 1185 19

Indian cobra (Naja naja naja) venom obtained from three different geographical regions was studied in terms of electrophoretic pattern, biochemical and pharmacological activities. SDS-PAGE banding pattern revealed significant variation in the protein constituents of the three regional venoms. The eastern venom showed highest indirect hemolysis and hyaluronidase activity. In contrast, western and southern venoms were rich in proteolytic activity. All the three regional venoms were devoid of p-tosyl-L-arginine methyl ester hydrolysing activity. The eastern venom was found to be most lethal among the three regional venoms. The lethal potency varied as eastern > western > southern regional venoms. In addition, all the three regional venoms showed marked variations in their ability to induce symptoms/signs of neurotoxicity, myotoxicity, edema and effect on plasma coagulation process. Polyclonal antiserum prepared against the venom of eastern region cross-reacted with both southern and western regional venoms, but varied in the extent of cross-reactivity by ouchterlony immunodiffusion and ELISA.
...
PMID:Variations in biochemical and pharmacological properties of Indian cobra (Naja naja naja) venom due to geographical distribution. 1193 52

The high molecular weight arylamidase-alkaline phosphatase-complex from rat kidney microsomes [1] was carefully dissociated by means of treatment with several hydrolytic enzymes or by acidification. Trypsin, chymotrypsin and pronase cause a selective solubilization of the enzymes discernible at their different electrophoretic mobility in polyacrylamide gel. The lower migrating zone represents phosphatase, the faster migrating zone shows arylamidase activity (molecular weights 180,000 and 172,000, respectively). Incubation of the complex with papain, lipase, neuraminidase or hyaluronidase and incubation at acid conditions (pH optimum 5.0) in the absence of any enzyme also yields in the appearance of two protein bands. In contrast to the alkaline hydrolases the acid hydrolases, the pH 5-treatment and with a certain degree also the lipase liberate a second arylamidase zone lying in the phosphatese containing zone during polyacrylamide gel electrophoresis. Treatment with SDS and subsequent SDS-polyacrylamide gel electrophoresis also results in a dissociation of the complex, but only in one protein fragement (approx, molecular weight 205,000).
...
PMID:??? 1194 35


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

---