Muscle tissue binding

Rabbit muscle homogenate binding Muscle tissue binding dominates all tissue binding and muscle binding in rabbit and human is similar Fraction unbound in muscle homogenate by dialysis [25]... 

Research in this area advanced in the 1970 s as several groups reported the isolation of potent toxins from P. brevis cell cultures (2-7). To date, the structures of at least eight active neurotoxins have been elucidated (PbTx-1 through PbTx-8) (8). Early studies of toxic fractions indicated diverse pathophysiological effects in vivo as well as in a number of nerve and muscle tissue preparations (reviewed in 9-11). The site of action of two major brevetoxins, PbTx-2 and PbTx-3, has been shown to be the voltage-sensitive sodium channel (8,12). These compounds bind to a specific receptor site on the channel complex where they cause persistent activation, increased Na flux, and subsequent depolarization of excitable cells at resting... 

Walsh The kinase binds to actin in the isolated state with a Kj of about 0.8 //M and to myofilaments with a Kof about 0.1 /tM. No measurements of the on- and off-rates have been made, however. In situ, most importantly, MLCK appears to be permanently bound since it does not dissociate from detergent-treated smooth muscle tissues, implying that the off-rate in situ is extremely slow or zero. 

Use of soy protein products in brine injected or absorbed whole muscle meat products such as beef, poultry, and seafood is reviewed. The importance of functionality on brine performance and within muscle tissue is stressed. Major considerations are selection of the proper soy protein, accompanying functionalities such as water-binding, gelling and viscosity, the specific meat system and requirements pertaining to nutrition, processing and marketing. 

This nonextractable radioactivity was probably the result of covalent binding of the furazolidone intermediates to endogenous macromolecules. The bioavailability of these bound tissue residues from the above pig residue depletion study was determined by feeding rats lyophilized samples of liver and muscle tissues from animals sacrificed at 0 and 45 days after the last treatment (132). Results showed that the fraction of the bound residues bioavailable to rats was in the range 16-41%. The toxicological impact of these bioavailable bound residues has not been yet determined. 

Apart from differences between muscle tissues from various parts of an animal, there are qualitative and quantitative differences in composition between animal species. Therefore, analytical methods will always have lo be tested on material from each individual species, since differences in fat composition, in the presence of species-specific proteins, and in colored components such as in the case of myoglobin in poultry and beef may influence both the extraction and the separation of the analytes. As an example, a recovery higher than 70% was obtained for furazolidone after spiking chicken and veal calf muscle tissue but only 10% after spiking pork tissue (16). In this study, the recovery from pork meat could markedly be improved by addition to the aqueous exfraction solvent of about 25% acetonitrile, an observation indicating binding of furazolidone to pork-specific proteins. 

Ivermectin binds to chloride ion channels in parasitic nerve and muscle cells, thereby increasing membrane permeability to chloride. Increased intracellular chloride results in hyperpolarization of nerve and muscle tissues, which results in paralysis and death of the parasite. Ivermectin is well tolerated during shortterm use in mild-to-moderate infections. Administration in more severe infections may cause swollen or tender lymph glands, fever, skin rash, itching, and joint and muscle pain, but these reactions may be... 

The classic example of competitive inhibition is inhibition of succinate dehydrogenase, an enzyme, by the compound malonate. Hans Krebs first elucidated the details of the citric acid cycle by adding malonate to minced pigeon muscle tissue and observing which intermediates accumulated after incubation of the mixture with various substrates. The structure of malonate is very similar to that of succinate (see Figure 1). The enzyme will bind malonate but cannot act further on it. That is, the enzyme and inhibitor form a nonproductive complex. We call this competitive inhibition, as succinate and malonate appear to compete for the same site on the enzyme. With competitive inhibition, the percent of inhibition is a function of the ratio between inhibitor and substrate, not the absolute concentration of inhibitor. 

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