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Antibody Detection of Venom Protein Variation within a Population of the Rattlesnake Crotalus v. viridis Ver este material de antemano
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Antibody Detection of Venom Protein Variation within a Population of the Rattlesnake Crotalus v. viridis

Autor: Michael Anaya; Eppie D Rael; Carl S Lieb; John C Perez; Richard J Salo
Edición/Formato: Artículo Artículo : Inglés (English)
Publicación:Journal of Herpetology, Dec., 1992, vol. 26, no. 4, p. 473-482
Base de datos:JSTOR
Otras bases de datos: British Library Serials
Resumen:
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Detalles

Tipo de documento: Artículo
Todos autores / colaboradores: Michael Anaya; Eppie D Rael; Carl S Lieb; John C Perez; Richard J Salo
ISSN:0022-1511
Número OCLC: 480331841
Nota del idioma: English
Notas: Fig. 1. Map of extreme western Texas and adjoining regions of southern New Mexico and Mexico indicating the source localities for specimens of Crotalus v. viridis. The solid circles with number correspond to venom samples (Cv) given in the Appendix; the half-filled symbol indicates the origin of the putative C. viridis × scutulatus natural hybrid described by Murphy and Crabtree (1988). HM and HB mark the approximate geographic centers of the Hueco Mountains and Hueco Bolson, respectively. The shaded area represents the geographic range of C. scutulatus in the study area, as inferred from museum specimens (UTEP) and other distributional data. The 1500 m contour line has been shown in order to emphasize the correlation of upland habitats to the restricted regional distribution of C. scutulatus; C. viridis is distributed throughout the area of the map where appropriate habitat occurs.
Fig. 2. Isoelectric focusing of C. v. viridis venoms stained with Coomassie blue. Outside lanes represent isoelectric point markers. Specimens are identified in Appendix 1. S denotes the Sigma venom.
Fig. 3. Isoelectric focusing immunoblots of C. v. viridis venoms, developed with monoclonal antibodies (A) CA-P-8 (for hemorrhagic toxin) and (B) CSS20 (for L-amino acid oxidase). The outside lanes contain isoelectric point markers stained with Coomassie blue. Specimens are identified in Appendix 1. S denotes the Sigma venom.
Fig. 4. SDS-PAGE (without 2-mercaptoethanol) of C. v. viridis venoms stained with Coomassie blue. Outside lanes contain the molecular weight markers. Venom sample numbers correspond to Cv samples in Appendix 1. S denotes the Sigma venom.
Fig. 5. Immunoblots of C. v. viridis venoms from gels described in Fig. 4. A, developed with monoclonal antibody CA-P-8 (for hemorrhagic toxin); B, with polyclonal antibody AF5 (for anti-complement protease); C, with monoclonal antibody CSS20 (for L-amino acid oxidase). Outside lanes contain the molecular weight markers stained with Coomassie blue; venom sample numbers correspond to Cv samples in Appendix 1. S denotes the Sigma venom.
Fig. 6. PAGE of C. v. viridis venom samples in 20% homogeneous gels without SDS or 2-mercaptoethanol. The gel was stained with Coomassie blue. The sample numbers correspond to the Cv samples given in Appendix 1. S denotes the Sigma venom.
Fig. 7. Immunoblots of C. v. viridis venoms from gel described in Fig. 6. A, developed with monoclonal antibody CA-P-8 (for hemorrhagic toxin); B, with monoclonal antibody CSS20 (for L-amino acid oxidase); C, with polyclonal antibody AF5 (for anticomplement protease). Venom sample numbers correspond to the Cv samples given in Appendix 1. S denotes the Sigma venom.
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Resumen:

As a preliminary investigation into intra-population variation in venom proteins in the prairie rattlesnake, Crotalus v. viridis, we analyzed a small number (11) of venom samples from extreme western Texas and adjoining New Mexico by electrophoresis and Western blotting methods. A monoclonal antibody raised against hemorrhagic toxin in C. atrox venom (CA-P-8) recognized all the venoms, but none was recognized by a monoclonal antibody raised against a hemorrhagic toxin in C. m. molossus venom (CMM-1). All the venoms were recognized by an anti-L-amino acid oxidase (CSS20) monoclonal antibody, but none was recognized by an anti-Mojave toxin antibody (CSS12). An antibody (AF5) against a protease in C. s. scutulatus venom that inactivates complement recognized all the venoms except the venom from one young snake. The principal individual venom differences were in the amounts of various venom components, although qualitative differences were noted. The principal similarities lie in the molecular weights of most of the venom proteins. Intrapopulational mobility differences were more pronounced in venom proteins separated by isoelectric focusing and PAGE without SDS and 2-mercaptoethanol.

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