Disrupted protein

Hypothermia—Indirect cryodestruction Metabolic uncoupling Energy deprivation Ionic imbalance Disruption of acid-base balance Waste accumulation Membrane phase transitions Cytoskeletal disassembly Frozen State—Direct cryodestruction Water solidification Hyperosmolality Cell-volume disruption Protein denaturation Tissue shearing Intracellular-ice propagation Membrane disruption Microvascular Thawed State Direct effects... 

Detergents disrupt protein-lipid and protein-protein interactions and play a large role in gel electrophoresis.59 60 SDS is the most common detergent used in PAGE... 

Bernards R (1991) N-myc disrupts protein kinase C-mediated signal transduction in neuroblastoma. EMBO J 10 1119-1125... 

For large-scale analysis, this strategy has been further modified for use in the array method (Ito et al., 2000 Uetz et al., 2000 Walhout et al., 2000). Such analyses in Sachromyces cerevisiae and Caenorhabditis elegans have already reported many potential interactions that need to be confirmed by further biological experimentation. Finally, another modification of the yeast two-hybrid system has been recently reported, termed reverse two-hybrid (Vidal and Endoh, 1999). This technique is being used to identify compounds and peptides that can disrupt protein-protein interactions and thus have an effect on various signaling pathways. 

No deaths. Disrupted protein metabolism in gills and kidneys... 

Enzyme reactions. Some toxicants can act as enzymes. A number of natural toxicants operate in this way. For example, snake venoms often contain hydrolytic enzymes, which degrade tissue. Ricin from the castor oil plant is more sophisticated and causes the hydrolytic destruction of ribosomes, so disrupting protein synthesis. 

Chlorophyll is a nonpolar molecule so it is soluble in most organic solvents. Acetone disrupts protein-pigment complexes (see Experiment 8). A more efficient extraction could be achieved if several extractions were carried out and the extracts pooled. 

Living arrays Yeast colonies expressing GAL4 fusion proteins Yeast colonies with transposon disruptions protein—protein and protein—DNA/RNA interactions phenotype analysis... 

Pipe, S. W., Saenko, E. L., Eickhorst, A. N., Kemball-Cook, G. and Kaufman, R. J. (2001). Hemophilia A mutations associated with 1-stage/ 2-stage activity discrepancy disrupt protein-protein interactions within the triplicated A domains of thrombin-activated factor Villa. Blood 97, 685-691. 

Equation (9.1) allows us in principle to draw a spectrum that matches the entire spectrum obtained experimentally. This is correct only if the recorded spectrum originates from one fluorophore (i.e., Trp in solution) or from compact protein within a folded structure. However, when the experimental spectrum originates from two fluorophores (i.e., mixtures of tyrosine and tryptophan in solution) or from a disrupted protein that has two classes of Trp residues, the calculated spectrum using Equation (9.1) does not match the recorded spectrum. 

The dramatic role of the anion can perhaps best be appreciated from simple quantitative considerations. In the absence of a suitable anion, specific binding of iron to transferrin does not occur at all the effective binding constant is zero. At physiologic pH and bicarbonate concentrations, however, the effective binding constant is about 5 X 1023 M"1 24, 50). This means that in 1 L of blood plasma, in which the transferrin is only about 30% saturated with iron, there will be less than one free ferric ion or that a molecule of the ferric—transferrin complex will spontaneously dissociate only about once in 10,000 years. Since iron is readily removed from the transferrin molecule during its interaction with the reticulocyte without disrupting protein structure 51, 52), a... 

Denaturating agents, which disrupt protein-protein interactions, as well as secondary and tertiary structures within proteins. 

We began this review with the question that led to the discovery of dysbindin-1, namely what disrupted protein interactions of dystrobrevin may help account for the cognitive deficits in Duchenne and Becker muscular dystrophy The discovery of dysbindin-1 has not led to an answer to that question, but has led to the discovery that abnormalities in the DTNBP 1 gene or in levels of its protein product do affect cognition in normal individuals and in schizophrenia cases. Establishing the mechanisms responsible for that effect is perhaps the most important topic of future basic and translational research on dysbindin-1. 

The impact of aerobic exercise on protein requirements remains uncertain. Exercise clearly can disrupt protein metabolism, both protein turnover and amino acid oxidation. However, it remains to be determined if these effects are acute effects of exhaustive exercise or if moderate exercise in trained individuals still produces increased oxidation of amino acids. 

Following cell lysis, or tissue disruption, proteins become exposed to a new and unphysiological environment, in which they need to be protected against processes of inactivation, denaturation or degradation (Coligan et al. 1995). Inactivation and denaturation are often a consequence of inadequate buffering lysis usually leads to a reduction of the pH of the medium as a result of active metabolism (e.g., glycolysis), which should be corrected by addition of ammonia or Tris solution. 

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