Binding proteins, purification

Berni, R., M. Stoppini and M.C. Zapponi. The piscine plasma retinol-binding protein. Purification, partial amino acid sequence and interaction with mammalian transthyretin. Eur. J. Biochem. 204 99-106, 1992. 

Growth hormone receptor and serum binding protein Purification, cloning and expression. Nature 330, 537-543. 

Leung D W, Spencer S A, Cachianes G, et al. (1987). Grouth hormone receptor and serum binding protein Purification, cloning and expression. Nature. 330 537-543. 

Dutta-Roy, A.K., Alpha-tocopherol-binding proteins purification and characterization, Methods Enzymol. 282, 278-297, 1997. 

Sonenberg, N., Rupprecht, K. M., Hecht, S. M., and Shatkin, A. J., 1979, Eukaryotic mRNA cap binding protein Purification by affinity chromatography on Se-pharose-coupled m GDP, Proc. Natl. Acad. Sci. USA 76 4345. 

The general transcription factor TFllD is believed to be the key link between specific transcription factors and the general preinitiation complex. However, the purification and molecular characterization of TFllD from higher eucaryotes have been hampered by its instability and heterogeneity. All preparations of TFllD contain the TATA box-binding protein in combination with a variety of different proteins called TBP-associated factors, TAFs. When the preinitiation complex has been assembled, strand separation of the DNA duplex occurs at the transcription start site, and RNA polymerase II is released from the promoter to initiate transcription. However, TFIID can remain bound to the core promoter and support rapid reinitiation of transcription by recruiting another molecule of RNA polymerase. 

Charbonneau, H., and Cormier, M. J. (1979). Ca2+-induced bioluminescence in Renilla reniformis. Purification and characterization of a calcium-triggered luciferin-binding protein. J. Biol. Chem. 254 769-780. 

Inouye, S., et al. (1989). Overexpression and purification of the recombinant calcium-binding protein, apoaequorin./. Biochem. 105 473-477. 

Guidon, P.T. Hightower, L.E. (1986). Purification and initial characterization of the 71-kilodalton rat heat-shock protein and its cognate as fatty acid binding proteins. Biochemistry, 25, 3231-9. 

Rauser, W.E. (1984). Isolation and partial purification of cadmium-binding protein from roots of the grass Agrostis gigantea. Plant Physiology, 74, 1025-9. 

Fig. 9 Purification of ELPs by ITC is based on the reversible inverse phase transition. Le/i Protein purification via direct ELP fusions. A soluble ELP fused to a target protein becomes reversibly insoluble upon increasing temperature above 7,. Center Protein purification via ELP coaggregation. An excess of free ELPs enhances the aggregation of trace quantities of ELP-fusions. Right Purification via ELP-mediated affinity capture (EMAC). ELPs are fused to capture proteins, which bind specifically and reversibly to a target protein. This target protein can then be aggregated at temperatures above the T,. Adapted from [38] with permission from Elsevier, copyright 2010...

Martel, R.R. and Law, J.H., Purification and properties of an ommochrome-binding protein from the hemolymph of the tobacco homworm, Manduca sexta, J. Biol. Chem., 266, 21392, 1991. 

For reasons that are not yet clear, skeletal muscle transverse (T)-tubule membranes contain 50-100-fold more high affinity DHP receptors than any other source yet identified [43,45]. Transverse tubule membranes contain 30-70 pmol/mg protein of DHP receptors that bind [ H]PN 200-100 with a of 0.1-0.2nM. The strategy utilized for the purification of L-type channels was similar to that used for the purification of other high affinity ligand binding proteins, and its success was predicted from the prior use of such an approach for the purification of other ion channels [54,55]. Thus the L-type channels were purified as high affinity DHP receptors, with the anticipation that the purified component(s) would constitute functional Ca channels. 

Ponnazhagan, S., and Kwon, B. S. (1992). A cis-acting element involved in mouse tyrosinase gene expression and partial purification of its binding protein. Pigment Cell Res. 5 155-161. 

DuVal GE, Fowler BA. 1989. Preliminary purification and characterization studies of a low molecular weight, high affinity cytosolic lead-binding protein in rat brain. Biochem Biophys Res Commun 159 177-184. 

Z. E. Jouni and M. Wells, Purification of a carotenoid-binding protein from the midgut of the silkworm, Bombyx mori, Ann. N. Y. Acad. Sci. 691 (1993) 210-212. 

M. R. Lakshman and M. N. Rao, Purification and characterization of cellular carotenoid-binding protein from mammalian liver, Methods Enzymol. 299 (1999) 441 -56. 

Fujii, H., Matsui, T., Tochihara, S., and Kawaguchi, Y. 1988b. Purification of carotenoids binding protein from larval hemolymph of the yellow blood strain of Bombyx mori. J. Seric. Sci. Jpn., 57(5) 398-404. 

Jouni, Z. E. and Wells, M. A. 1996. Purification and partial characterization of a lutein-binding protein from the midgut of the silkworm Bombyx mori. J. Biol. Chem., 271(25) 14722-14726. 

Kennedy, M.C., Mende-Mueller, L., Blondin, G.A., and Beinert, H. 1992. Purification and characterization of cytosolic aconitase from beef hver and its relationship to the iron-responsive element binding protein. Proceedings of the National Academy of Sciences of the USA 89 11730-11734. 

Moebius, F.F., Hanner, M., Knaus, H.G., Weber, F., Striessnig, J., and Glossmann, H. (1994) Purification and amino-terminal sequencing of the high affinity phenylalkylamine Ca2+ antagonist binding protein from guinea pig liver endoplasmic reticulum./. Biol. Chem. 269, 29314-29320. 

COPI-coated vesicles mediate intra-Golgi transport and Golgi to ER retrograde transport. The coats of these vesicles do not show the geometric forms seen with clathrin coats and have a more complex protein composition [3]. Coat protein purification first lead to the identification of a complex composed of seven individual coat-protein subunits, known as COPI or coatomer. Some of these subunits bear a sequence similarity to clathrin adaptors. In addition, there is a small GTP-binding protein, Arfl, present on COPI-coated vesicles. 

---