Protein factor, soluble

HELMINGER, J., RAUSCH, T HILGENBERG, W., A soluble protein factor from Chinese cabbage converts indole-3-acetaldoxime to IAA, Phytochemistry, 1987, 26, 615-618. 

Kofoed, K., et al. (2007) Use of plasma C-reactive protein, procalcitonin, neutrophils, macrophage migration inhibitory factor, soluble urokinase-type plasminogen activator receptor, and soluble triggering receptor expressed on myeloid cells-1 in combination to diagnose infections a prospective study. Crit Care. 11, R38. 

During the course of the symposium, several dietary factors that can influence xenobiotic metabolism were discussed in detail. Here we will attempt t summarize in the broadest terms how various classic nutrient groups might exert an influence on xenobiotic metabolism. For convenience, the dietary groups have been broken into carbohydrates, lipids, proteins, water-soluble vitamins, fat-soluble vitamins and trace elements. It is difficult to take any one group individually, and it must be kept in mind that the interactions are continuous and extremely complicated. 

Marinova, Z., Yakovleva, T., Meltzig, M., Hallberg, M., Nylander, I., Ray, K., Rodgers, D. W., Hauser, K. F., Ekstrom, T. J., and Bakalkin, G. (2004). A novel soluble protein factor with non-opioid dynorphin A-binding activity. Biochem. Biophys. Res. Commun. 321, 202—209. 

The role of soluble protein factor in chloroplast electron transport. In Non-Heme Iron Proteins Role in Energy Conversion, A. San Pietro, ed., Antioch Press, Yellow Springs, Ohio, pp. 115—136 (1965). 

The aminoacyl transfer reaction, one of the latter stages in protein synthesis, involves incorporation of amino acids from soluble ribonucleic acid-amino acid into ribosomal protein. This reaction requires guanosine triphosphate and a soluble portion of the cell. Evidence has been obtained with rat liver preparations that aminoacyl transfer is catalyzed by two protein factors, aminoacyl transferases (or polymerases) I and n, which have been resolved and partially purified from the soluble fraction. Transferase n activity has also been obtained from deoxycholate-soluble extracts of microsomes. With purified transferases I and n, incorporation is observed with relatively low levels of GTP its sulfhy-dryl requirement is met by a variety of compounds. The characteristics of this purified amino acid incorporating system, in terms of dependency on the concentration of its components, are described. 

Surface plastnon resonance Association constant Dissociation constant Hexaethylene glycol spacer Sambucus nigra agglutinin High-mobility-group transcriptional factor Soluble green fluorescent protein Calmodulin... 

Synaptosomal proteins are involved in synaptic transmission, which is deranged in AD. The machinery consists of synaptosomal proteins, including soluble N-ethylmaleimide-sensitive factor attachment proteins (SNAPs) present as three isoforms, a, (3 and y, synaptosomal-associated protein 25 (SNAP 25), synapto-tagmin, and vesicular proteins. Proteomics studies showed reduced expression... 

Yoo, B. C., Cairns, N., Fountouiakis, M., Lubec, G. (2001a). Synaptosomal proteins, beta-soluble N-ethylmaleimide-sensitive facTor attadiment protein (beta-SNAP), gamma-SNAP and synaptotagmin I in brain of patients with Down syndrome and Alzheimer s disease. Dement. Geriatr. Cogn. Disord. 

It is now well established that in vivo efficient membrane fusion requires the interaction of small cytoplasmically exposed membrane proteins called soluble N-ethylmaleimide sensitive factor (NSF) attachment receptors (SNAREs) (Sollner et al., 1993). For synaptic vesicle exocytosis, the relevant SNAREs are synaptobrevin/ vesicle-associated membrane protein (VAMP) 1 and 2, syntaxin 1, and synaptosome-associ-ated protein of 25,000 daltons (SNAP-25). Synaptobrevins/ VAMPs are localized primarily on synaptic vesicles, while syntaxin and SNAP-25 are localized primarily on the plasma membrane. Fusion is driven by the progressive zippering of vesicle and plasma membrane SNAREs forming a four-helix bundle (Sutton et al., 1998). Although many other proteins appear to play critical roles in synaptic vesicle exocytosis, it seems likely that SNAREs are the minimal machinery required for fusion (Weber et al., 1998). Once assembled, SNARE complexes are disassembled by NSF, which functions in conjunction with SNAP proteins. 

Fisher CJ> Agosti JM Jr, Opal SM, et al. Treatment of septic shock with the tumor necrosis factor receptor Fc fusion protein. The Soluble TNF Receptor Sepsis Study Group. N Engl J Medl996 334 1697-702. 

The role of the cytoplasmic effectors is obscure since their effects disappear when the enzyme is solubilized by Triton X-100. The possible participation of the soluble protein factor (SPF) as a carrier for substrate inside the membrane has been explored (Chapter 3). The SPF has been shown not only to stimulate the conversion of externally added squalene and oxidosqualene but also to activate squalene epoxidase as well as 2,3-oxidosqualene cyclase when the substrate is membrane bound [85,86]. SPF has been purified and shown to promote the transfer of squalene from one population of microsomes to another [87,88]. Nevertheless, SPF has no... 

Lantz, M., Gullberg, U., Nilsson, E., and Olsson, 1. Characterization in vitro of a human tumor necrosis factor-binding protein. A soluble form of a tumor necrosis factor receptor. J. Clin. Invest. 86, 1396-1342 (1990). 

Solubility is due to the native structure of proteins. In soluble proteins, hydrophilic parts are located on the outside of the molecule, and the hydrophobic regions are buried. Denaturation induces the insolubility of a protein. According to Bigelow [115], two structural features, hydrophobicity and charge frequency, are the major factors that control the solubility of proteins. 

Mechanics of protein translation. Protein translation begins with the activated amino acids and proceeds in three stages initiation, elongation and termination. At each stage, the driving energy is provided by GTP hydrolysis and specific soluble protein factors participate in the processes which take place on ribosomes (Ramakrishnan,... 

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