title: Proteolysis of interleukin-2, interferon and immunoglobulin by venoms.
abstract: Limited proteolysis by venoms was analysed by the cleaved peptide band(s) in SDS-polyacrylamide gel electrophoresis. The venom from Crotalus atrox degraded interferon, interleukin-2, IgG, IgM, and a crude form of acetyl cholinesterase but had no effect on IgA. Although the venom from Androctonus australis did not exert appreciable proteolysis on any of the immunoglobulins it had potent proteolytic activities against interferon and interleukin-2. The venom from Vespula maculifrons had only a minor proteolytic effect on interferon. The proteolysis by venoms was not effectively inhibited by alpha 1-antitrypsin or a2-macroglobulin. Moreover, no appreciable proteolytic activity was detected in the venoms from Bufo arenarum, Apis mellifera and Heloderma suspectrum.
authors.affiliation: Division of Science and Mathematics, Bethune-Cookman College, Daytona Beach, Florida 32115.
authors.forename: W N
authors.initials: WN
authors.lastname: Kuo
authors.forename: U
authors.initials: U
authors.lastname: Ganesan
authors.forename: A
authors.initials: A
authors.lastname: Robinson
authors.forename: J R
authors.initials: JR
authors.lastname: Flanders
authors.forename: M E
authors.initials: ME
authors.lastname: Fausti
authors.forename: M N
authors.initials: MN
authors.lastname: Jean
authors.forename: M L
authors.initials: ML
authors.lastname: Gurnee
authors.forename: J
authors.initials: J
authors.lastname: Kuo
mesh_terms: D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000378:metabolism*; D006801:Humans; D007074:Immunoglobulin G / Q000378:metabolism*; D007372:Interferons / Q000378:metabolism*; D007376:Interleukin-2 / Q000378:metabolism*; D051379:Mice; D014688:Venoms / Q000378:metabolism*
chemical_list: D007074:Immunoglobulin G; D007376:Interleukin-2; D014688:Venoms; D007372:Interferons; D010450:Endopeptidases