GMBS

Rotenone-containing iasecticides have been used as dusts of ground roots, dispersible powders, and emulsive extracts. Their principal uses have been for appHcation to edible produce just prior to harvest and for the control of animal ectoparasites and cattle gmbs. 

Avermectins and Ivermectin. The avermectias are pentacycHc lactones isolated from fermentation products of Streptomjces avermitilis and ivermectin is a semisynthetic chemical, 22,23-dihydroavermectia (46). Ivermectin is effective in very low doses for the control of red spider mites on deciduous fmits, in baits for the control of imported fire ants, and as a parasiticide for Onchocerca volvulus in humans and for catde gmbs. These insecticides appear to function as agonists for the neuroinhibitory transmitter y-aminobutyric acid (GABA) (see Antiparasitic agents, avermectins). 

Ivermectin is used in cattle, sheep and horses at 0.2 mg/kg swine at 0.3 mg/kg dogs at 0.006 mg/kg and man at 0.05 —0.2 mg/kg. It is effective against parasitic nematodes, gmbs, Hce, mites, ticks, and bots. Ivermectin is not active against tapeworms, flatworms, bacteria, or fungi. 

GMBS can be used in multi-step conjugation protocols wherein an amine-containing molecule or protein is first modified via the NHS ester end (its most labile-reactive group)to... 

Figure 5.8 The reaction of GMBS with an amine-containing molecule yields a maleimide-activated intermediate that then can be used to crosslink with a sulfhydryl-containing compound.

GMBS or sulfo-GMBS have been used for studying carnitine palmitoyltransferase-1 in its formation of a complex within the outer mitochondrial membrane (Faye et al., 2007), for investigating protein organization of the postsynaptic density (Liu et al., 2006), and in studying the structure and dynamics of rhodopsin (Jacobsen et al., 2006). 

The protocol for using GMBS or sulfo-GMBS in protein-protein crosslinking applications is similar to that of SMCC or sulfo-SMCC (see Section 1.3, this chapter). 

Figure 1. Scale drawing of glass plates. BSA was adsorbed into the left position (2.5 cm long) of the plates, which subsequently was the cathodal end. After electrophoresis the plates were cut up into 4 equal pieces, each 3.5 cm long (numbered 1 to 4) for Y-counting plus an anodal end (H), used for handling, which remained uncounted. Reproduced from Absolom et al. (8) with permission from Verlag Chemie Gmb H.

Isotherm of BSA adsorption on ethanol-cleaned glass, with plateaus at 1.8 g/cm and at 2.6 pg/cm. Reproduced from Absolom et al. (8) with permission from Verlag Chemie Gmb H. 

Soares GMB, Costa-Ferreira M, Pessoa de Amorim MT (2001) Decolorization of an anthra-quinone type dye using a laccase formulation. Bioresour Technol 79 171... 

Soares GMB, Amorim MTP, Hrdina R, Costa-Ferreira M (2002) Studies on the biotransformation of novel disazo dyes by laccase. Process Biochem 37 581-587... 

Dialyze an antibody solution against Soln. C and concentrate to 20-30 mg/ml. Add 3 mg of sulfo-SMCC (3-sulfosuccinimidyl-4-(N-maleimidomethyl)-cyclohexane-l-caboxylate, Mr 436.7) or of sulfo-GMBS (N-(y-maleimidobutyryloxy)-3-sulfo-N-hydroxysuc-cinimide ester, Mr 382.3), dissolved in ddH20 to 60 mg/ml, to 10 mg of antibody, rock at RT for 15 min and add further 3 mg of coupling reagent. Desalt on a Sephadex G-25 column, equilibrated with Soln. A, after total incubation time of 30 min and use the activated antibody (protein) for conjugation immediately (see above). 

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