Protein release mechanical

Park, T. G., Lee, H. Y., and Nam, Y. S. (1998), A new preparation method for protein loaded poly(D,L-lactic-co-glycolic acid) microspheres and protein release mechanism study, J. Controlled Release, 55,181-191. 

Table 4.2 Overview of the protein release mechanisms from hydrogels. Reproduced from [114],...

Tm 48°C respectively). This is consistent with a reduction step aiding heme release by weakening the complex prior to, or during, the actual release of heme effected by the hemopexin receptor. (The nondestructive mode of transport by hemopexin with recycling of intact protein demands mechanisms to reversibly lower the affinity of the complex.) With or without NaCl, lowering the pH from 7.4 to 6.5 has little effect... 

Fig. 6. Biochemo-mechanically controlled protein release using urease-loaded gel. The experiment was carried out in a 0.2 M ammonium buffer maintained at 35 °C using insulin (Mw = 5733) as the protein solute. (E. Kokufuta, S. Matsukawa, T. Ebihara, and K. Mat-suda [77])...

The sequence analysis of the /3-lactamase protein of B. licheniformis 749/C was performed on both the extracellular and the cell-bound enzyme (of. serial Nos. 5 and 6, Table I). The slight differences between the two forms were confined to the N-terminus and attributed to the difference in the release mechanism. Peptides corresponding to about 90% of the molecule have been characterized and their sequences combined to form five larger fragments. 

Regulation of Adenylate Cyclase and Neurotransmitter Release - Protein Phosphorylation Mechanisms... 

The mechanical properties of single hydrated dextran microcapsules (< 10 pm in diameter) with an embedded model protein drug have also been measured by the micromanipulation technique, and the information obtained (such as the Young s modulus) was used to derive their average pore size based on a statistical rubber elasticity theory (Ward and Hadley, 1993) and furthermore to predict the protein release rate (Stenekes et al., 2000). 

Cells must ensure that each newly synthesized protein is sorted to its correct location where it can carry out the appropriate function. This process is called protein targeting. In a eukaryotic cell, the protein may be destined to stay in the cytosol, for example an enzyme involved in glycolysis (see Topic J3). Alternatively it may need to be targeted to an organelle (such as a mitochondrion, lysosome, peroxisome, chloroplast or the nucleus) or be inserted into the plasma membrane or exported out of the cell. In bacteria such as E. coli, the protein may stay in the cytosol, be inserted into the plasma membrane or the outer membrane, be sent to the space between these two membranes (the periplasmic space) or be exported from the cell. In both prokaryotes and eukaryotes, if a protein is destined for the cytosol, it is made on free ribosomes in the cytosol and released directly into the cytosol. If it is destined for other final locations, specific protein-targeting mechanisms are involved. 

Mitochondrial pathway of caspase activation has been demonstrated in various experimental models and humans to contribute significantly to car-diomyocyte apoptosis in the heart [41-44], Studies suggest that mitochondrial-mediated apoptosis contributes to cardiomyocyte loss through intermembrane space proteins release, Bcl-2 protein involvement, and procaspase activation [41, 45, 46], Due to the energy required by heart muscle, mitochondria are particularly abundant in cardiomyocytes. Under physiological conditions, prosurvival mechanisms exist to protect the myocardium from inappropriately triggered apoptosis [3],... 

D2R causes a potentiation of calcium-evoked arachidonic acid release through G-protein-dependent mechanisms involving PKC in a range of cells (Felder et al., 1991 Kanterman et al., 1991 Piomelli et al., 1991 Nilsson et al., 1998). 

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