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)

In order to determine the proteins of major allergenic importance in honeybee venom (Apis mellifera) it was chromatographed on G-50 Sephadex. The four major protein peaks eluted were identified as hyaluronidase, phospholipase, melittin, and apamin. Testing these preparations on the leukocytes of 6 honeybee-sensitive patients, with the in vitro method of histamine release, revealed that all individuals were most sensitive to phospholipase A. IgE antibodies against phospholipase A (RAST) were found in the sera of honeybee-sensitive patients and IgG antibodies to this venom component were found in the sera from beekeepers and venom-treated patients. Melittin appeared to be allergenic in several patients, but the results were variable and were possibly due to contamination with phospholipase. All patients were insensitive to the hyaluronidase and apamin preparations. We conclude that phospholipase A is the major allergen of honeybee venom and, since this protein is readily available, it should be useful for diagnostic and therapeutic studies as well as for the standardization of materials used in the management of honeybee-sensitive patients.
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PMID:Allergy to insect stings. II. Phospholipase A: the major allergen in honeybee venom. 5 82

Chromatography of honeybee venom on Sephadex G-150 super fine revealed a high molecular weight (HMW) fraction that elutes prior to hyaluronidase (HYAL) and comprises 2% to 4% of the venom weight. HMW appears to exist in polymeric form, and the polymer which is present in greatest concentration has an estimated molecular weight of 105,000 D. The 12% nitrogen content of HMW suggests it may not be all protein. HMW is antigenically and enzymatically distinct from HYAL and phospholipase A2 (PHOS A). The acid phosphatase activity known to be present in honeybee venom was found in the HMW fraction. Since it reacts by RAST with the sera of most individuals known to be sensitive to honeybee venom, and releases histamine from the peripheral leukocytes of such individuals, its role as an allergen is confirmed. Since individuals react to different degrees to HMW, HYAL, and PHOS A, there does not appear to be a single principal allergen in honeybee venom.
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PMID:A high molecular weight allergenic fraction of honeybee venom. 7 Apr 36

Two new allergenic specificites were detected in honeybee venom and the two corresponding protein substances isolated by gel filtration, immunoadsorption, and ion exchange chromatography. The first of these, allergen B, has a molecular weight ranging from 49,000 to more than 200,00 d and can be recognized by rabbit and guinea pig antisera as well as by human reaginic sera using the radioallergosorbent test (RAST). Allergen B gives a single line in immunodiffusion distinct from hyaluronidase, phospholipase A, melittin, and the other high molecular weight substances described and gives a single band at 49,000 d in sodium dodecyl sulfate (SDS) polyacrylamide gel. The second substance, allergen C, has a molecular weight of 105,000 d and was separated from allergen B by immunoadsorption with insoluble antibody. Allergen C was shown to be distinct from the other sustances in bee venom by immunodiffusion with animal antisera. One human reaginic serum was monospecific for allergen C. Two other minor components of 86,000 and 71,000 d are present in bee venom; their allergenic activities are unknown. The two specifities, B and C, comprise most of the reactivity of the previously described Sephadex G-75 fraction 1 and clearly are important allergens, reacting with 98% of sera from bee venom-allergic individuals.
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PMID:Allergens in bee venom II. Two new high molecular weight allergenic specificities. 40 40

The mammalian toxicity of the potently algogenic venom of the ant Pogonomyrmex badius is greater than that reported for any other insect venom. This enzyme-rich venom contains high concentrations of phospholipase A2 and B, hyaluronidase, acid phosphatase, lipase, and esterases. This hemolytic secretion from the poison gland products unusual symptoms in mammals and appears to have been evolved as a deterrent for vertebrate predators.
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PMID:A harvester ant venom: chemistry and pharmacology. 65 54

The use of honeybee venoms and their components may assist in the elucidation of the pathophysiology of reactions to honeybee stings. This initial study compared venoms from various sources by chemical and biological assays, and significant variations were observed. Ten different bee venoms were compared by nitrogen analysis, mouse toxicity, hyaluronidase content, and antigenicity. Based on mouse toxicity, hyaluronidase content, and gel diffusion analysis, two groups of bee venoms could be differentiated. Venoms in one group, Group A, were more toxic, contained hyaluronidase, and showed an additional precipitin band. All venoms contained mellitin as a major fraction, which formed nonimmune precipitin bands during gel diffusion analysis. Gel filtration chromatography and dialysis separated the venoms into components that were then identified by enzyme assays, rat mast cell degranulation, hemolytic activity, and gel diffusion analysis. The venoms within Group A showed similar components, some of which, most noticeably hyaluronidase, were not present in Group B. Dialysis showed that a large portion of the venom could pass through a cellophane membrane including a portion of the phospholipase A. Heterogeneous molecular weights were found for phospholipase A by both gel filtration and dialysis, and may reflect variation in carbohydrate content. It appears that bee venom variability for whatever reason, a heterogeneous MW antigen, and a non-immune precipitable component require careful consideration in any study involving this venomm. These studies have yielded relatively pure, identified bee venom components which can be employed in further studies investigating reactions to honeybee stings.
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PMID:Comparison of honeybee venoms and their components from various sources. 80

Honeybee venom was separated into seven fractions by gel filtration on Sephadex G-75. Allergenic activities of these fractions were assessed by the paper disc radioallergosorbent test (RAST) with a panel of sera from 24 individuals who had systemic reactions to bee stings, 7 who had large local reactions, and 10 control subjects who had reactions of 5 cm or less following bee stings. Three fractions were identified by enzyme or direct hemolytic activity. Twenty-nine of 31 sera from patients having either systemic or large local reactions to bee stings were positive when radioallergosorbent tested with whole bee venom; 22 were positive to phospholipase A, and 28 were positive to both fractions 1 and 2. Thirteen sera combined most strongly with fraction 1, 12 sera most strongly with fraction 2, hyaluronidase, and three sera about equally with fractions 1, 2, and 3. Reactions with other fractions were much weaker. Fractions 1 and 2 were potent inhibitors of RAST with whole venom in the sera reacting most strongly with fractions 1 or 2, respectively. Fraction 3, phospholipase A, and commercial bee venom phospholipase A were significantly less potent inhibitors with the sera tested. In the cases in which IgE antibody bindings to fractions 1, 2, and 3 were of similar magnitude, inhibitions of RAST using the various fractions both on the discs and as inhibitors demonstrated substantial cross-reactivity between the fractions. These results strongly indicate that by using RAST with human sera from bee sting-sensitive individuals, fraction 1, the high molecular materials, and fraction 2, hyaluronidase, are the major allergens in honeybee venom. Phospholipase A appears to be of secondary importance.
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PMID:Allergens in bee venom. I. Separation and identification of the major allergens. 97 62

1. The enzymatic, hemorrhagic, procoagulant and anticoagulant activities of venoms of some animals including snakes, lizards, toads, scorpions, spider, wasps, bees and ants were compared. 2. Snake venom was the richest source of enzymes among the animal venoms. Most other animal venoms were devoid of phosphodiesterase, L-amino acid oxidase, alkaline phosphomonoesterase and acetylcholinesterase activities and only a few exhibited arginine ester hydrolase activity. These venoms, however, exhibited wide ranges of protease, 5'-nucleotidase and hyaluronidase activities. Most of the animal venoms examined exhibited some phospholipase A activity. 3. Other than snake venoms, only venoms of the toad Bufo calamita and the lizards were hemorrhagic, and only venoms of the social wasps, social bees and harvester ant exhibited strong anticoagulant activity. Procoagulant activity occurs only in snake venoms.
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PMID:Comparative study of the enzymatic, hemorrhagic, procoagulant and anticoagulant activities of some animal venoms. 136 Mar 87

Using immunoblot studies, detailed antibody patterns were performed with the sera of 10 yellow jacket allergic patients undergoing specific immunotherapy with a yellow jacket venom SQ-depot extract (ALK, Denmark). Five males and five females (age range 10-65, mean 48 years) were investigated. All patients had a history of systemic reactions after an insect sting and a positive skin-prick test at a dose of at least 100 micrograms/ml yellow jacket venom. Yellow jacket venom (ALK) was separated on a 7.5-20% SDS-PAGE, transferred to nitrocellulose (NC), and then the NC-strips were incubated with the patients' sera. For detection of IgE, IgG, IgG1 and IgG4, an alkaline phosphatase linked 2nd antibody was used. Prior to immunotherapy, a strong IgE binding was detected at 25 kD in nine of 10 patients, representing Antigen-5 (Ag-5) as major allergen. Reactivity to this antigen was also present with the other immunoglobulin classes, although not as marked. In addition, a second frequent IgG and IgG1-binding band was seen at 35 kD (phospholipase A). Only weak or no binding to this band was found with IgE and IgG4. Binding to hyaluronidase (43 kD) was seen only in three cases. During immunotherapy, a significant increase in IgG and particularly IgG4 staining was found with Ag-5, whereas hyaluronidase induces mainly an IgG1 response and phospholipase A showed only a weak IgG response. In addition, the formation of new IgG4 binding to proteins in the region of about 70-90 kD was found in most patients. The dose necessary for the induction of this antibody formation was greater than or equal to 150.00 SQ yellow jacket venom.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:IgE, IgG, IgG1 and IgG4 patterns in yellow jacket allergic patients during immunotherapy with a venom depot extract. 157 21

1. The biological properties of nine venom samples from six taxa of Micrurus were investigated. The venoms exhibited low protease, phosphodiesterase and 5'-nucleotidase activities, moderate to strong phospholipase A and hyaluronidase activities, variable L-amino acid oxidase activity and were devoid of arginine ester hydrolase and thrombin-like activities. Some venom samples exhibited strong acetylcholinesterase activity. Venoms of M. c. dumerili and M. frontalis exhibited exceptionally high alkaline phosphomonoesterase activity while two of the M. f. fulvius venom samples tested exhibited strong hemorrhagic activity in mice. 2. The polyacrylamide gel electrophoretic patterns of the venoms indicate that most of the Micrurus venom proteins are basic proteins. All Micrurus venoms tested exhibited similar SDS-polyacrylamide gel electrophoretic patterns, with an intense low mol. wt protein band. 3. The Micrurus venoms appear to exhibit biological properties similar to other elapid venoms found in Asia and Africa. There are, however, no common characteristics in the biological properties of the venoms examined at the generic level.
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PMID:The biological properties of venoms of some American coral snakes (Genus micrurus). 158 85

1. The hemorrhagic, procoagulant, anticoagulant, protease, arginine ester hydrolase, phosphodiesterase, alkaline phosphomonoesterase, 5'-nucleotidase, hyaluronidase, phospholipase A and L-amino acid oxidase activities of 50 venom samples from 20 taxa of rattlesnake (genera Crotalus and Sistrurus) were examined. 2. The results show that notwithstanding individual variations in the biological activities of Crotalus venoms and the wide ranges of certain biological activities observed, there are some common characteristics at the genus and species levels. 3. The differences in biological activities of the venoms compared can be used for differentiation of the species. Particularly useful for this purpose are the thrombin-like enzyme, protease, arginine ester hydrolase, hemorrhagic and phospholipase A activities and kaolin-cephalin clotting time measurements.
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PMID:A comparative study of the biological activities of rattlesnake (genera Crotalus and Sistrurus) venoms. 167 59


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