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Antihemorrhagic

The Experts below are selected from a list of 216 Experts worldwide ranked by ideXlab platform

Sarah Weissenberg – 1st expert on this subject based on the ideXlab platform

  • inhibition of the proteolytic activity of hemorrhagin e from crotalus atrox venom by antihemorrhagins from homologous serum
    Toxicon, 1992
    Co-Authors: Sarah Weissenberg, Michael Ovadia, Elazar Kochva

    Abstract:

    Abstract Antihemorrhagic proteins from Crotalus atrox serum were tested for their ability to inhibit the proteolytic activity of the hemorrhagic toxin-e from Crotalus atrox venom and of several other proteolytic enzymes: trypsin, collagenase and thermolysin. The Antihemorrhagic proteins inhibited the proteolytic activity of hemorrhagin-e when tested on gelatin type I and collagen type IV, the proteolytic activity of trypsin on photofilm gelatin and the proteolytic activity of whole venom when tested on azocollagen and photofilm gelatin. The antihemorrhagins failed to inhibit the proteolytic activity of trypsin when tested on the specific synthetic substrate N-acetyl- dl -phenylalanine-β-naphthyl ester (APNE), the activity of microbial collagenase on N-(3-[2-furyl]acryloyl)-Leu-Gly-Pro-Ala (FALGPA) or on azocollagen and the activity of thermolysin on N-(3-[2-furyl] acryloyl)-Gly-Leu amide (FAGLA). It is tentatively suggested that the antihemorrhagins from snake blood serum are proteinase inhibitors that under-went specialization towards the neutralization of the proteolytic activity of hemorrhagic toxins.

  • Antihemorrhagic factors from the blood serum of the western diamondback rattlesnake crotalus atrox
    Toxicon, 1991
    Co-Authors: Sarah Weissenberg, Michael Ovadia, Gideon Fleminger, Elazar Kochva

    Abstract:

    Abstract Several Antihemorrhagic factors isolated from C. atrox serum are glycoproteins with mol. wt ranging from 65,000 to 80,000. The Antihemorrhagic activity of these factors was stable at a pH range of 1.3–11.5 and at temperatures up to 85°C, for 30 min. The isolated antihemorrhagins also neutralized the proteolytic activity of C. atrox venom, as tested with azocollagen and gelatin, and formed a complex with hemorrhagic toxin e isolated from the same venom. The neutralization capacity of the isolated antihemorrhagins was six times as high as the commercial polyvalent antivenom produced for clinical use.

Elazar Kochva – 2nd expert on this subject based on the ideXlab platform

  • inhibition of the proteolytic activity of hemorrhagin e from crotalus atrox venom by antihemorrhagins from homologous serum
    Toxicon, 1992
    Co-Authors: Sarah Weissenberg, Michael Ovadia, Elazar Kochva

    Abstract:

    Abstract Antihemorrhagic proteins from Crotalus atrox serum were tested for their ability to inhibit the proteolytic activity of the hemorrhagic toxin-e from Crotalus atrox venom and of several other proteolytic enzymes: trypsin, collagenase and thermolysin. The Antihemorrhagic proteins inhibited the proteolytic activity of hemorrhagin-e when tested on gelatin type I and collagen type IV, the proteolytic activity of trypsin on photofilm gelatin and the proteolytic activity of whole venom when tested on azocollagen and photofilm gelatin. The antihemorrhagins failed to inhibit the proteolytic activity of trypsin when tested on the specific synthetic substrate N-acetyl- dl -phenylalanine-β-naphthyl ester (APNE), the activity of microbial collagenase on N-(3-[2-furyl]acryloyl)-Leu-Gly-Pro-Ala (FALGPA) or on azocollagen and the activity of thermolysin on N-(3-[2-furyl] acryloyl)-Gly-Leu amide (FAGLA). It is tentatively suggested that the antihemorrhagins from snake blood serum are proteinase inhibitors that under-went specialization towards the neutralization of the proteolytic activity of hemorrhagic toxins.

  • Antihemorrhagic factors from the blood serum of the western diamondback rattlesnake crotalus atrox
    Toxicon, 1991
    Co-Authors: Sarah Weissenberg, Michael Ovadia, Gideon Fleminger, Elazar Kochva

    Abstract:

    Abstract Several Antihemorrhagic factors isolated from C. atrox serum are glycoproteins with mol. wt ranging from 65,000 to 80,000. The Antihemorrhagic activity of these factors was stable at a pH range of 1.3–11.5 and at temperatures up to 85°C, for 30 min. The isolated antihemorrhagins also neutralized the proteolytic activity of C. atrox venom, as tested with azocollagen and gelatin, and formed a complex with hemorrhagic toxin e isolated from the same venom. The neutralization capacity of the isolated antihemorrhagins was six times as high as the commercial polyvalent antivenom produced for clinical use.

John C. Perez – 3rd expert on this subject based on the ideXlab platform

  • Resistance of warm-blooded animals to snake venoms.
    Toxicon, 2002
    Co-Authors: John C. Perez, Willis C. Haws, Vivian E Garcia, Bruce M. Jennings

    Abstract:

    Abstract Crotalus atrox venom resistance in 40 species of animal sera was studied by means of Antihemorrhagic assay, ring precipitation test and serum protection test. The Antihemorrhagic titers ranged from 0 to 256 with 16 animal sera having a titer greater than two. Five animal sera precipitated with C. atrox venom and the titers ranged from 0 to 64. Procyon lotor (racoon), Liomys irroratus (Mexican spiny pocket mouse) and two species of Peromyscus sp. (white footed deer mouse) were the only unimmunized animals with both a positive Antihemorrhagic and ring precipitation titer. One of the resistant sera, Neotoma micropus (gray woodrat), was further studied to determine effects of five other snake venoms. Neotoma micropus serum neutralized hemorrhagic factors in all hemorrhagic venoms tested but would not neutralize the lethal factors of elapid venoms in the serum protection test. It appears that both reptiles and warm-blooded animals have Antihemorrhagic factors in their sera.

  • Comparative study on hemorrhagic and proteolytic activities of snake venoms.
    Toxicon, 2002
    Co-Authors: Shyi Yi Huang, John C. Perez

    Abstract:

    Abstract The hemorrhagic and proteolytic titers of nine snake venoms were measured. Suitable venom dilutions were selected to study the Antihemorrhagic and antiproteolytic activities of three warm-blooded animal sera — gray woodrat (Neotoma micropus), hispidus cottonrat (Sigmodon hispidus) and Virginia opossum (Didelphis virginiana). It was demonstrated that all hemorrhagic venoms are proteolytic. The results show that the hemorrhagic activity of the venoms is readily neutralized by the sera; however, the proteolytic activity is not neutralized. We suggest that the mechanisms involved in neutralizing the two activities are not closely related.

  • the effects of western diamondback rattlesnake crotalus atrox venom on the production of antihemorrhagins and or antibodies in the virginia opossum didelphis virginiana
    Toxicon, 2002
    Co-Authors: Morgan R Mckeller, John C. Perez

    Abstract:

    Abstract Opossums are animals that are naturally resistant to the proteolytic effects of Crotalid venoms. Opossums possess proteinase inhibitors in their sera that bind to and neutralize hemorrhagic and other proteolytic activity in many snake venoms. The proteinase inhibitors are not antibodies since they have different molecular weights (60 kDa) and pI (4.2). The purpose of this study was to determine if opossums were capable of producing antibodies against venom and/or increasing the production of proteinase inhibitors (specifically antihemorrhagins). Five different venom immunization protocols were used to determine the effects of the venom in the opossums. The dosages ranged from 1 mg of venom per immunization to 350 mg/kg body weight of venom per immunization. The Antihemorrhagic response was increased, but there is no evidence to suggest that an opossum can produce antibodies against venom. The lack of an antibody response is most likely due to the natural proteinase inhibitors clearing the venom from the opossum’s body before an antibody response can occur.