@article {524,
	title = {Influence of chelation and oxidation state on vanadium bioavailability, and their effects on tissue concentrations of zinc, copper, and iron},
	journal = {Biological Trace Element Research},
	volume = {86},
	number = {1},
	year = {2002},
	note = {ISI Document Delivery No.: 541ZTTimes Cited: 27Cited Reference Count: 45},
	month = {Apr},
	pages = {31-44},
	type = {Article},
	abstract = {Today, vanadium compounds are frequently included in nutritional supplements and are also being developed for therapeutic use in diabetes mellitus. Previously, tissue uptake of vanadium from bis(maltolato)oxovanadium(IV) (BMOV) was shown to be increased compared to its uptake from vanadyl sulfate (VS). Our primary objective was to test the hypothesis that complexation increases vanadium uptake and that this effect is independent of oxidation state. A secondary objective was to compare the effects of vanadium complexation and oxidation state on tissue iron, copper, and zinc. Wistar rats were fed either ammonium metavanadate (AMV), VS, or BMOV (1.2 mM each in the drinking water). Tissue uptake of V following 12 wk of BMOV or AMV was higher than that from VS (p < 0.05). BMOV led to decreased tissue Zn and increased bone Fe content. The same three compounds were compared in a cellular model of absorption (Caco-2 cells). Vanadium uptake from VS was higher than that from BMOV or AMV at 10 min, but from BMOV (250 \&mu;M only, 60 min), uptake was far greater than from AMV or VS. These results show that neither complexation nor oxidation state alone are adequate predictors of relative absorption, tissue accumulation, or trace element interactions.},
	keywords = {ABSORPTION, BIS(MALTOLATO)OXOVANADIUM(IV), bone, CACO-2, Caco-2 cells, COMPLEXES, DIABETIC RATS, GLUCOSE-METABOLISM, IN-VITRO, INSULIN, kidney, ORTHO-VANADATE, skeletal muscle, SULFATE, VANADIUM, zinc},
	isbn = {0163-4984},
	url = {<Go to ISI>://000175018100004},
	author = {Thompson, K. H. and Tsukada, Y. and Xu, Z. M. and Battell, M. and McNeill, J. H. and Orvig, Chris}
}
@article {4489,
	title = {Analysis of gamma-carboxyglutamic acid content of protein, urine, and plasma by capillary electrophoresis and laser-induced fluorescence},
	journal = {Analytical Chemistry},
	volume = {71},
	number = {8},
	year = {1999},
	note = {ISI Document Delivery No.: 186XUTimes Cited: 12Cited Reference Count: 32},
	month = {Apr},
	pages = {1633-1637},
	type = {Article},
	abstract = {When the properties of an analyte are known, the separation system can be designed to make the analyte of interest migrate at either a much faster ora much slower velocity compared to other molecules in the sample matrix. A simple and sensitive method to analyze the gamma-carboxyglutamic acid (Gla) content of protein, urine, and plasma was developed using capillary electrophoresis with laser-induced fluorescence detection (CE-IIF), The separation method is designed according to the specific properties of three amino acids of interest. The number of Gla residues from three vitamin K-dependent proteins were estimated by quantifying the amount of fluorescein thiocarbamyl derivative of Gla after alkaline hydrolysis and fluorescein isothiocyanate labeling. Human prothrombin, blood coagulation factor X, and bovine osteocalcin were calculated to have 10.0 +/- 0.7, 11.0 +/- 0.6, and 2.1 +/- 0.1 Gla residues. per mole of protein, respectively, which agreed well with amino acid sequencing data. The analysis of free Gla content in urine and plasma was also demonstrated by this method. It was demonstrated that submicrograms of protein can be characterized by CE-LIF.},
	keywords = {bone, CLINICAL-SIGNIFICANCE, GLUTAMIC-ACID, MARKERS, PROTHROMBIN, SERUM, VITAMIN-K},
	isbn = {0003-2700},
	url = {<Go to ISI>://000079756900025},
	author = {Britz-McKibbin, P. and Vo, H. C. and MacGillivray, R. T. A. and Chen, D. D. Y.}
}
