@article {5118,
	title = {Arsenic speciation in sea scallop gonads},
	journal = {Applied Organometallic Chemistry},
	volume = {15},
	number = {6},
	year = {2001},
	note = {ISI Document Delivery No.: 435TUTimes Cited: 15Cited Reference Count: 19},
	month = {Jun},
	pages = {533-538},
	type = {Article},
	abstract = {The arsenic species in male and female sea scallop gonads (Placopecten magellanicus) at pre-spawning and post-spawning stages, collected near Newfoundland, Canada, were characterized by using high-performance liquid chromatography-inductively coupled plasma-mass spectrometry, All samples contain arsenobetaine (0.5-3.0 mug g(-1)) and a dimethylarsinoylriboside derivative as the major water-soluble arsenic compounds. Male pre-spawning gonads contain 0.35-2.4 mug g(-1) of the dimethylarsinoylriboside, Female pre-spawning gonads contain 0.47-9.64 mug g(-1) of the same compound. Postspawning gonads, both male and female, contain higher concentrations of this compound (3.7-11.4 mug g(-1)). The total concentrations of water-soluble arsenic compounds are different in male and female pre-spawning gonads. These differences are not obvious in post-spawning gonads. Post-spawning gonads contain higher total concentrations of water-soluble arsenic compounds than pre-spawning gonads. Copyright (C) 2001 John Wiley \& Sons, Ltd.},
	keywords = {arsenic, arsenobetaine, arsenosugar, HEPATOCYTES, HPLC, ICP-MS, MONOMETHYLARSONOUS ACID, RAT, scallops, SPECIATION},
	isbn = {0268-2605},
	url = {<Go to ISI>://000168897900012},
	author = {Lai, V. W. M. and Cullen, W. R. and Ray, S.}
}
@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.}
}
