@article {1176,
	title = {New insights into the interactions of serum proteins with bis(maltolato)oxovanadium(IV): Transport and biotransformation of insulin-enhancing vanadium pharmaceuticals},
	journal = {Journal of the American Chemical Society},
	volume = {127},
	number = {14},
	year = {2005},
	note = {ISI Document Delivery No.: 914LQTimes Cited: 39Cited Reference Count: 66},
	month = {Apr},
	pages = {5104-5115},
	type = {Article},
	abstract = {Significant new insights into the interactions of the potent insulin-enhancing compound bis(maltolato)oxovanadium(IV) (BMOV) with the serum proteins, apo-transferrin and albumin, are presented. Identical reaction products are observed by electron paramagnetic resonance (EPR) with either BMOV or vanadyl sulfate (VOSO4) in solutions of human serum apo-transferrin. Further detailed study rules out the presence of a ternary ligand-vanadyl-transferrin complex proposed previously. By contrast, differences in reaction products are observed for the interactions of BMOV and VOSO4 with human serum albumin (HSA), wherein adduct formation between albumin and BMOV is detected. In BMOV-albumin solutions, vanadyl ions are bound in a unique manner not observed in comparable solutions Of VOSO4 and albumin. Presentation of chelated vanadyl ions precludes binding at the numerous nonspecific sites and produces a unique EPR spectrum which is assigned to a BMOV-HSA adduct. The adduct species cannot be produced, however, from a solution Of VOSO4 and HSA titrated with maltol. Addition of maltol to a VOSO4-HSA solution instead results in formation of a different end product which has been assigned as a ternary complex, VO(ma)(HSA). Furthermore, analysis of solution equilibria using a model system of BMOV with 1-methylimidazole (formation constant log K = 4.5(1), by difference electronic absorption spectroscopy) lends support to an adduct binding mode (VO(ma)(2)-HSA) proposed herein for BMOV and HSA. This detailed report of an in vitro reactivity difference between VOSO4 and BMOV may have bearing on the form of active vanadium metabolites delivered to target tissues. Albumin binding of vanadium chelates is seen to have a potentially dramatic effect on pharmacokinetics, transport, and efficacy of these antidiabetic chelates.},
	keywords = {BINDING CONSTANTS, COMPLEXES, DEPENDENT DIABETES-MELLITUS, ELECTRON-PARAMAGNETIC RESONANCE, HUMAN SEROTRANSFERRIN, IN-VIVO, IRON REMOVAL, METALLOKINETIC ANALYSIS, MIMETIC AGENT, TRANSFERRIN},
	isbn = {0002-7863},
	url = {<Go to ISI>://000228229600036},
	author = {Liboiron, B. D. and Thompson, K. H. and Hanson, G. R. and Lam, E. and Aebischer, N. and Orvig, Chris}
}
@article {3984,
	title = {On-line monitoring and control of methanol concentration in shake-flask cultures of Pichia pastoris},
	journal = {Biotechnology and Bioengineering},
	volume = {56},
	number = {3},
	year = {1997},
	note = {ISI Document Delivery No.: XZ728Times Cited: 48Cited Reference Count: 19},
	month = {Nov},
	pages = {279-286},
	type = {Article},
	abstract = {The methylotrophic yeast Pichia pastoris can be used to express recombinant genes at high levels under the control of the methanol-inducible alcohol oxidase 1 (AOX1) promoter. Accurate regulation of the methanol concentration in P. pastoris cultures is necessary to maintain induction, while preventing accumulation of methanol to cytotoxic levels. We developed an inexpensive methanol sensor that uses a gas-permeable silicone rubber tube immersed in the culture medium and an organic solvent vapor detector. The sensor was used to monitor methanol concentration continuously throughout a fed-batch shake-flask culture of a P. pastoris clone producing the N-lobe of human transferrin. The sensor calibration was stable for the duration of the culture and the output signal accurately reflected the methanol concentration determined off-line by HPLC. A closed-loop control system utilizing this sensor was developed and used to maintain a 0.3\% (v/v) methanol concentration in the culture. Use of this system resulted in a fivefold increase in volumetric protein productivity over levels obtained using the conventional fed-batch protocol. (C) 1997 John Wiley \& Sons, Inc.},
	keywords = {fermentation, GENE-EXPRESSION, methanol monitoring and control, methanol sensor, methylotrophic yeast, Pichia pastoris, PROTEINS, SEMICONDUCTOR GAS SENSORS, shake-flask cultures, TRANSFERRIN, YEAST},
	isbn = {0006-3592},
	url = {<Go to ISI>://A1997XZ72800005},
	author = {Guarna, M. M. and Lesnicki, G. J. and Tam, B. M. and Robinson, J. and Radziminski, C. Z. and Hasenwinkle, D. and Boraston, A. and Jervis, E. and MacGillivray, R. T. A. and Turner, R. F. B. and Kilburn, D. G.}
}
@article {3223,
	title = {EVIDENCE FOR ENERGY-DEPENDENT TRANSPORT OF ALUMINUM OUT OF BRAIN EXTRACELLULAR FLUID},
	journal = {Toxicology},
	volume = {98},
	number = {1-3},
	year = {1995},
	note = {ISI Document Delivery No.: QX943Times Cited: 22Cited Reference Count: 36},
	month = {Apr},
	pages = {31-39},
	type = {Article},
	abstract = {Aluminum (Al) can cause CNS toxicity. The mechanism of its blood-brain barrier (BBB) permeation is poorly understood. In this study, microdialysis was used to determine extracellular fluid (ECF) unbound aluminum distribution between frontal cortex (FC) and blood during steady-state aluminum concentrations. The brain/blood aluminum ratio was determined. Over a 16-fold range of aluminum concentrations (dosed as aluminum citrate), brain/blood aluminum ratios were 0.10-0.15, consistently and significantly <1. Aluminum diffusion cannot account for these results, suggesting the presence of a carrier that moves aluminum out of brain extracellular fluid. These aluminum brain/blood ratios (BBRs) were not significantly different over the range of concentrations studied, suggesting an inability to saturate the carrier. Brain/blood aluminum ratios obtained with four aluminum-hydroxypyridinones were also significantly <1 (0.1-0.3), and were generally significantly different among themselves and from the aluminum citrate BBR. Movement of a BBB permeability marker from blood into brain extracellular fluid suggested partial BBB opening. The aluminum BBRs obtained (all much less than 1), in the presence of a partially opened BBR, suggest an efficient carrier moving aluminum out of brain ECF. Addition of cyanide to the brain microdialysis probe solution significantly increased the Al (citrate) BBR to 1, These results suggest the presence of an efficient, energy-dependent carrier that removes aluminum from brain ECF, either into brain cells or blood.},
	keywords = {aluminum, ANTIPYRINE, BARRIER, BLOOD, BLOOD-BRAIN BARRIER, CHELATORS INVITRO, COMPLEXES, ENERGY-DEPENDENT ACTIVE TRANSPORT, INVIVO MICRODIALYSIS, iron, MICRODIALYSIS, MOBILIZATION, permeability, TRANSFERRIN},
	isbn = {0300-483X},
	url = {<Go to ISI>://A1995QX94300004},
	author = {Allen, D. D. and Orvig, Chris and Yokel, R. A.}
}
