@article {2845,
	title = {HORSE PLASMA GELSOLIN LABELED WITH FLUORESCEIN ISOTHIOCYANATE RESPONDS TO CALCIUM AND ACTIN},
	journal = {European Journal of Biochemistry},
	volume = {212},
	number = {3},
	year = {1993},
	note = {ISI Document Delivery No.: KT704Times Cited: 7Cited Reference Count: 26},
	month = {Mar},
	pages = {713-718},
	type = {Article},
	abstract = {Reaction between horse plasma gelsolin and fluorescein-5-isothiocyanate (FITC) resulted in incorporation of 4.8 +/- 0.6 fluorescein groups/gelsolin molecule. The sites of modification were not clustered in any one portion of the gelsolin polypeptide chain; all major peptides produced by proteolytic digestion with alpha-chymotrypsin exhibited a fluorescence characteristic of fluorescein. FITC-gelsolin has a peptide-backbone circular dichroism spectrum at 20-degrees-C that is indistinguishable from that of native gelsolin, but FITC-gelsolin is considerably more resistant than native gelsolin to thermally induced precipitation. FITC-gelsolin is fully able to carry out severing of F-actin filaments, the prime function of gelsolin in plasma. An opening up of the structure of gelsolin on binding Ca2+ is evident from an increased susceptibility of FITC-gelsolin to quenching by I-. Ca2+ dependence of the interaction between gelsolin and actin is evident in titrations both of intensity and polarization of the fluorescence of FITC-gelsolin solutions. A Ca2+-sensitive interaction between gelsolin and tropomyosin also is observed.},
	keywords = {BINDING DOMAIN, FILAMENTS, PROTEIN, TROPOMYOSIN},
	isbn = {0014-2956},
	url = {<Go to ISI>://A1993KT70400010},
	author = {Koepf, E. K. and Burtnick, L. D.}
}
@article {7284,
	title = {INTERACTION OF PLASMA GELSOLIN WITH TROPOMYOSIN},
	journal = {Febs Letters},
	volume = {309},
	number = {1},
	year = {1992},
	note = {ISI Document Delivery No.: JL068Times Cited: 20Cited Reference Count: 17},
	month = {Aug},
	pages = {56-58},
	type = {Article},
	abstract = {Horse plasma gelsolin labelled with benzophenone-4-isothiocyanate can be photochemically cross-linked to rabbit cardiac tropomyosin. The cross-linking proceeds with greater efficiency in calcium-containing buffers. Further evidence for interaction between these proteins is provided by retention of fluorescently labelled gelsolin on tropomyosin-agarose affinity columns and by the ability of tropomyosin to cause an increase in the fluorescence intensity of gelsolin labelled with fluorescein-5-isothiocyanate. Both of these effects require the presence of calcium ions.},
	keywords = {actin, FILAMENTS, gelsolin, MUSCLE, PROTEIN, TROPOMYOSIN},
	isbn = {0014-5793},
	url = {<Go to ISI>://A1992JL06800013},
	author = {Koepf, E. K. and Burtnick, L. D.}
}
@article {7358,
	title = {MONOMER AND EXCIMER FLUORESCENCE OF HORSE PLASMA GELSOLIN LABELED WITH N-(1-PYRENYL)IODOACETAMIDE},
	journal = {Biochemistry and Cell Biology-Biochimie Et Biologie Cellulaire},
	volume = {70},
	number = {7},
	year = {1992},
	note = {ISI Document Delivery No.: JP667Times Cited: 3Cited Reference Count: 27},
	month = {Jul},
	pages = {573-578},
	type = {Article},
	abstract = {Horse plasma gelsolin was labelled with the sulfhydryl-specific fluorescent reagent N-(1-pyrenyl)iodoacetamide. The level of incorporation of probe was 1.6 +/- 0.3 mol pyrene/mol gelsolin. The circular dichroism spectrum of pyrenyl-gelsolin and its ability to interact with muscle actin were not different from that found for unmodified gelsolin. The emission from pyrenyl-gelsolin was dominated by a broad emission band centred near 483 nm, characteristic of the presence of pyrene excimers. Analysis of excitation spectra for the monomer and excimer-type fluorescence suggested that ground-state interactions may occur between adjacent pyrenes in the gelsolin structure. In the case either of excimer formation or of ground-state pyrene-pyrene interactions in doubly labelled gelsolin molecules, the modified Cys residues must be in close proximity in the folded protein structure. Thermal denaturation of gelsolin could be monitored by observing the decrease in excimer emission that accompanied heating and unfolding of the tertiary structure. While heat treatment alone did not eliminate excimer fluorescence, digestion of gelsolin with chymotrypsin completely abolished such emission. Also, pyrenyl-gelsolin prepared and studied in 6 M guanidine-HCl exhibited fluorescence characteristic of pyrene monomers exclusively.},
	keywords = {ACTIN-FILAMENTS, BINDING, CIRCULAR-DICHROISM, denaturation, FLUORESCENCE LIFETIME, gelsolin, POLYMERIZATION, PROBE, PROTEIN, PYRENE EXCIMER FLUORESCENCE, PYRENE-ACTIN, STATE, thermal, TROPOMYOSIN},
	isbn = {0829-8211},
	url = {<Go to ISI>://A1992JP66700008},
	author = {Silva, B. E. R. and Koepf, E. K. and Burtnick, L. D. and Turro, N. J.}
}
@article {7352,
	title = {STABILIZATION OF THE STRUCTURE OF HORSE PLASMA VITAMIN-D BINDING-PROTEIN BY DISULFIDE BONDS},
	journal = {Biochemistry and Cell Biology-Biochimie Et Biologie Cellulaire},
	volume = {70},
	number = {1},
	year = {1992},
	note = {ISI Document Delivery No.: HG742Times Cited: 1Cited Reference Count: 27},
	month = {Jan},
	pages = {10-15},
	type = {Article},
	abstract = {Vitamin D binding protein (DBP) was isolated from horse plasma in a four-step procedure that involved Affi-Gel Blue affinity chromatography, gel filtration, hydroxylapatite chromatography, and anion exchange high-pressure liquid chromatography. The yield of DBP from 80 mL of plasma was 6-7 mg. Horse plasma DBP closely resembles other plasma DBPs, being a tryptophan-free protein of M(r) 53 000. It is able to bind to and block the polymerization of monomeric actin. The secondary structure of DBP was calculated from circular dichroism measurements to be 39\% alpha-helix, 42\% beta-sheet, and 19\% random coil. Circular dichroism and fluorescence studies revealed that the disulfide bonds of DBP contribute substantial structural stabilization to the molecule with respect to thermal denaturation. The thermal stability of DBP can be used to advantage. Incorporation of a brief treatment at 70-degrees-C into the preparative scheme enables omission of one chromatographic step, without detectable alteration of the purified product.},
	keywords = {actin, circular dichroism, CIRCULAR-DICHROISM, COMPLEX, denaturation, DISULFIDE BONDS, FLUORESCENCE, GC-GLOBULIN, POLYMERIZATION, RAT, SERUM, thermal, TROPOMYOSIN, VITAMIN-D BINDING PROTEIN},
	isbn = {0829-8211},
	url = {<Go to ISI>://A1992HG74200002},
	author = {Robinson, R. C. and Burtnick, L. D.}
}
