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Androctonus australis

An attempt is being made to find crystals of an arthropod hemocyanin which diffract to high resolution and have identical subunits in the asymmetric unit. To that end Buisson et al. (1989) crystallized subunit Aa6 of Androctonus australie hemocyanin in two forms one which diffracts only to 8 A and one which diffracts to 3 A. [Pg.174]

Figure 17. Schematic diagrams of some representative topologically chiral proteins.79 (a) Condensed schematic drawing of the L subunit of the quinoprotein TV-MADH. The looped line represents the polypeptide backbone with N and C terminals. Cysteine (or half-cystine) residues are numbered, and their a-carbons are indicated by filled circles. Intrachain disulfide bonds are shown as dashed lines joining a pair of filled circles. The heavy line symbolizes an intrachain cofactor link, (b) Chromatium high potential iron protein (HiPIP), one of several Fe4S4 cluster-containing proteins, (c) Toxin II from the scorpion Androctonus australis Hector. Reprinted with permission from C. Liang and K. Mislow, J. Math. Chem. 1994,15,245. Copyright 1994, Baltzer Science Publishers. Figure 17. Schematic diagrams of some representative topologically chiral proteins.79 (a) Condensed schematic drawing of the L subunit of the quinoprotein TV-MADH. The looped line represents the polypeptide backbone with N and C terminals. Cysteine (or half-cystine) residues are numbered, and their a-carbons are indicated by filled circles. Intrachain disulfide bonds are shown as dashed lines joining a pair of filled circles. The heavy line symbolizes an intrachain cofactor link, (b) Chromatium high potential iron protein (HiPIP), one of several Fe4S4 cluster-containing proteins, (c) Toxin II from the scorpion Androctonus australis Hector. Reprinted with permission from C. Liang and K. Mislow, J. Math. Chem. 1994,15,245. Copyright 1994, Baltzer Science Publishers.
Clot-Faybesse, O., Juin, M., Rochat, H. and Devaux, C. (1999). Monoclonal antibodies against the Androctonus australis hector scorpion neurotoxin I characterisation and use for venom neutralisation. FEBS Lett., 458, 313-318. [Pg.370]

Fontecilla-Camps, J.-C., Habersetzer-Rochat, C. and Rochat, H. (1988). Orthorhombic crystals and three-dimensional structure of the potent toxin II from the scorpion Androctonus australis Hector. Proc. Natl. Acad. Sci. USA, 85, 7443-7447. [Pg.370]

Although being intensively investigated, only very few subunit types were sequenced of the 4 x 6-meric scorpion He (Androctonus australis, subunit Aa6 of eight subunit types ), and the 8 x 6-meric horseshoe crab L. polyphemus, subunit 11 of more than ten subunit types ). [Pg.979]

Contrasting to thanatin and lactoferricin B, tachyplesins [110,111] and polyphemusins [112,113], androctonin [114] from the scorpion Androctonus australis, gomesin from the spider Acanthoscurria gomesiana [115], protegrin from porcine leukocytes [117,118], and 7 -AMPl from the plant Impatiens balsamina [122], have four cysteine residues in their sequenees. They all fold into a double-stranded antiparallel P-sheet structure. [Pg.628]

EXAMPLE The minimum amount of Yellow Desert Scorpion (Androctonus Australis) venom required to effect an adult human is. oiioz(32omg). To determine how much of the venom is required to effect a rat, a diminutive creature, we consult the chart to find the percent of the average dose. The dose required to harm a diminutive creature is 1% of the average, or. oooiioz(3.2mg). [Pg.5]

E. californicum (4x6-mer) is in accordance with this theory the presence of carbohydrate in Androctonus australis (4x6-mer) He, however, is in contrast with it. The centipede Scutigera coleoptrata has an unusually high carbohydrate content (4.9%) for an arthropod He. The deviation of the chilopod He from the other arthropod Hcs is also reflected by the three-dimensional structure, which is composed of six hexamers [13]. [Pg.126]

N-linked carbohydrate chain from Androctonus australis hemocyanin [15]... [Pg.127]

Androctonus australis hector (Scorpion) Venom Toxin Aahl scFv Mouse Immune [99]... [Pg.863]

Devaux C, Moreau E, Goyffon M, et al. (2001). Construction and functional evaluation of a single-chain antibody fragment that neutralizes toxin Aahl from the venom of the scorpion Androctonus australis hector. Eur. J. Biochem. 268 694-702. [Pg.878]

Androctonus australis (AaTT, scorpion) AcNPV/BmNPV (38-40)... [Pg.352]

The Insect-Selective Neurotoxin, AalT. The North African scorpion, Androctonus australis Hector, possesses three classes of toxins in its venom. One of these classes is specific for insects although one anti-insect toxin has been shown to induce a response in both insect and mammalian systems (41). A. australis possess an insect toxin (AalT) which is a single chained polypeptide composed of seventy amino acids (Mr = 8kDa) cross linked by four disulfide bridges (42). The insect selectivity of AalT has been documented by toxicity, binding and electrophysiological assays (43), and studies with mice have shown that 50 mg/kg (subcutaneous) produced no adverse physiological symptoms (44). [Pg.354]


See other pages where Androctonus australis is mentioned: [Pg.194]    [Pg.280]    [Pg.69]    [Pg.357]    [Pg.140]    [Pg.15]    [Pg.76]    [Pg.126]    [Pg.126]    [Pg.362]    [Pg.341]    [Pg.27]    [Pg.190]    [Pg.278]    [Pg.59]    [Pg.380]    [Pg.37]    [Pg.447]   
See also in sourсe #XX -- [ Pg.357 , Pg.369 , Pg.370 ]

See also in sourсe #XX -- [ Pg.124 , Pg.126 , Pg.127 ]

See also in sourсe #XX -- [ Pg.23 , Pg.341 ]

See also in sourсe #XX -- [ Pg.341 ]




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