@article {2309,
	title = {Conformations of Gas-Phase Ions of Ubiquitin, Cytochrome c, Apomyoglobin, and beta-Lactoglobulin Produced from Two Different Solution Conformations},
	journal = {Journal of the American Society for Mass Spectrometry},
	volume = {19},
	number = {12},
	year = {2008},
	note = {ISI Document Delivery No.: 385IWTimes Cited: 2Cited Reference Count: 36Wright, P. John Zhang, Jianmin Douglas, D. J.},
	month = {Dec},
	pages = {1906-1913},
	type = {Article},
	abstract = {At low pH in solutions of 50\% methanol, proteins form expanded denatured states (the "H" state). In 90\% methanol, proteins form expanded helical denatured states with artificial alpha-helices (the "H-c" state). Gas-phase ions of ubiquitin, cytochrome c, apomyoglobin, and native and disulfide-reduced beta-lactoglobulin were formed by electrospray ionization (EST) of the proteins from the H and H-c states in solution. Both states in solution produce the same charge states in EST. The conformations of the ions were studied with cross section measurements and gas-phase H/D exchange experiments. The cross sections show that the ions retain considerable folded structure. For a given protein and given charge state, ions produced from the H and H-c states showed the same cross sections (within similar to 1\%). Ions of cytochrome c, apomyoglobin, and native and reduced beta-lactoglobulin of a given charge state showed no differences in H/D exchange level when produced from the H or H-c state. However, ubiquitin ions produced from the H-c state consistently exchange fewer (similar to 13\%) hydrogens than ions produced from the H state, suggesting that in this case the gas-phase protein ions retain some memory of their solution conformations. (J Am Soc Mass Spectrom 2008, 19, 1906-1913) (c) 2008 Published by Elsevier Inc. on behalf of American Society for Mass Spectrometry},
	keywords = {CIRCULAR-DICHROISM, COLLISION CROSS-SECTIONS, H/D EXCHANGE, HYDROGEN/DEUTERIUM EXCHANGE, IONIZATION MASS-SPECTROMETRY, MYOGLOBIN, OF-FLIGHT, PROTEIN IONS, STABILITY, SYSTEM, TRAP},
	isbn = {1044-0305},
	url = {<Go to ISI>://000261808900023},
	author = {Wright, P. J. and Zhang, J. M. and Douglas, D. J.}
}
@article {2307,
	title = {Cyanobacterial copper-binding ligands isolated from artificial seawater cultures},
	journal = {Marine Chemistry},
	volume = {110},
	number = {1-2},
	year = {2008},
	note = {ISI Document Delivery No.: 313BETimes Cited: 4Cited Reference Count: 34Wiramanaden, Cheryl I. E. Cullen, Jay T. Ross, Andrew R. S. Orians, Kristin J.},
	month = {May},
	pages = {28-41},
	type = {Article},
	abstract = {This paper demonstrates a method to isolate and characterise strong biogenic copper-binding ligands from an artificial seawater matrix. Pseudo-polarography is used to detect the ligands, determine their ionic strength-corrected binding constants, and track them through each step of the extraction process. Two ligand types are found, one strong and one relatively weak, with log K{\textquoteright} values of 49.4 +/- 1.1 and 19.8 +/- 5.5 respectively, assuming that the metal is bound as copper(II). If a copper(I) complex, the log K{\textquoteright} of the strong copper-binding ligand would be 25. Pseudo-polarography is then used to assess different resins for ligand extraction and to determine the eluent fraction in which the strong ligand is recovered. XAD-16 is found to be a suitable resin for extracting the strong binding ligand from salt water into methanol, suggesting that the ligand is weakly hydrophobic. As ligands are identified by their complexation of copper, no assumptions are made regarding the functional groups of these natural ligands. The copper-binding ligands are successfully extracted into solvents suitable for mass spectrometric analysis using soft ionisation methods such as electrospray and MALDI. (C) 2008 Elsevier B.V. All rights reserved.},
	keywords = {AFFINITY-CHROMATOGRAPHY, chemical speciation, COMPETITION TECHNIQUE, COMPLEXING LIGANDS, copper, CU STRESS, EMILIANIA-HUXLEYI, IONIZATION MASS-SPECTROMETRY, LIGANDS, mass, NORTH PACIFIC, ORGANIC-COMPLEXES, polarography, SARGASSO SEA, sea water, SPECTROMETRY, TRACE-METALS},
	isbn = {0304-4203},
	url = {<Go to ISI>://000256715300004},
	author = {Wiramanaden, C. I. E. and Cullen, J. T. and Ross, A. R. S. and Orians, K. J.}
}
@article {959,
	title = {Efficient synthesis of isotopically pure isotope-coded affinity tagging reagents},
	journal = {Bioconjugate Chemistry},
	volume = {15},
	number = {1},
	year = {2004},
	note = {ISI Document Delivery No.: 766UDTimes Cited: 7Cited Reference Count: 24},
	month = {Jan-Feb},
	pages = {224-230},
	type = {Article},
	abstract = {Synthesis of an isotopically pure d(8)-ICAT linker, N- [(5,5,6,6,8,8 9,9-H-2)-13-biotinamido-4,7,10-trioxatridecanyl] tert-butyloxy carbamide (12), has been achieved in seven steps with an overall yield of 33\%. Conjugation of exchange-inert d(4)-starting materials by classic etherification reaction yielded a pure synthon, carrying eight deuteriums that remained exchange-inert throughout subsequent reactions. This modified synthesis constitutes a significant improvement to the reported syntheses of "heavy" ICAT reagent in terms of expense, yield, and isotopic retention. This synthesis is easily adapted to incorporate additional deuterium atoms and is equally applicable for incorporation of either C-13 and/or O-18. In addition, this synthesis allows for the introduction of different orthogonal functionalities and provides for a high yielding series of differentially encoded ICAT tags.},
	keywords = {GEL-ELECTROPHORESIS, IONIZATION MASS-SPECTROMETRY, LIQUID-CHROMATOGRAPHY, PEPTIDES, PROTEINS, PROTEOME ANALYSIS, TAGS},
	isbn = {1043-1802},
	url = {<Go to ISI>://000188393200027},
	author = {Patel, A. and Perrin,David M.}
}
@article {827,
	title = {Using ellipsoids to model charge distributions in gas phase protein complex ion dissociation},
	journal = {Canadian Journal of Chemistry-Revue Canadienne De Chimie},
	volume = {82},
	number = {12},
	year = {2004},
	note = {ISI Document Delivery No.: 898JHTimes Cited: 12Cited Reference Count: 31},
	month = {Dec},
	pages = {1736-1744},
	type = {Article},
	abstract = {Gas phase protein complex dissociation was modelled using ellipsoids on which discrete charges were placed in randomly chosen charge sites. A number of sizes, shapes, orientations, and types of ellipsoids were considered. For each case, charge transfer parameters and electrostatic energies were calculated as a function of the fractional surface area. It was found that to within 10-15\%, the charge on product ions after dissociation is distributed according to their fractional surface area. This can imply, for example, that in experiments measuring the dissociation of homodimers, charge asymmetries of greater than 10-15\% in the product ions signal that one of the ions has greatly increased its surface area, such as would occur with unfolding. This assumes that proton transfer occurs on a timescale fast enough that the dissociation products adopt the minimum electrostatic energy configuration. Calculation of this energy shows that it is minimized when one or more of the monomers is in an extended conformation.},
	keywords = {charge asymmetry, CYTOCHROME-C, ELECTROSPRAY-IONIZATION, ellipsoid charge model, EXCHANGE, IONIZATION MASS-SPECTROMETRY, ORIGIN, protein complex dissociation},
	isbn = {0008-4042},
	url = {<Go to ISI>://000227072600011},
	author = {Csiszar, S. and Thachuk, M.}
}
@article {681,
	title = {Conformations of gas-phase lysozyme ions produced from two different solution conformations},
	journal = {Analytical Chemistry},
	volume = {75},
	number = {6},
	year = {2003},
	note = {ISI Document Delivery No.: 657PQTimes Cited: 15Cited Reference Count: 41},
	month = {Mar},
	pages = {1325-1330},
	type = {Article},
	abstract = {Near pH 2.0, lysozyme in water is in its native conformation, and in water/methanol (2/8) it adopts a helical denatured conformation (Kamatari et al. Protein Sci. 1998, 7, 681-688). Hydrogen/deuterium (H/D) exchange of lysozyme in solution confirms that it is partially unfolded at pH 2.0 in water/methanol (v/v = 2/8). With electrospray ionization (ESI) mass spectrometry (MS), lysozyme in water produces ions with charges +7 to +12, with the greatest intensity at +10, whereas lysozyme in water/methanol (2/8) produces ions with charges +6 to +12 with the greatest intensity at +7. Thus, lysozyme is an exception to the rule that a protein denatured in solution forms higher charge states than the same protein in its folded native conformations in solution. Because the same charge states are produced from these two solution conformations, a direct comparison of the properties of the gas-phase ions produced from two very different solution conformations is possible. The conformations of lysozyme ions in the gas phase were studied using cross section measurements and gas-phase H/D exchange. Similar cross sections and H/D exchange levels were observed for same-charge states of lysozyme ions formed from the native and helical denatured conformations in solution. Cross sections show that the ions have compact structures. Thus, disulfide-intact gaseous lysozyme ions generated from the denatured state in water/methanol (2/8) refold into compact structures in the gas phase on a time scale of milliseconds or less.},
	keywords = {COLLISION, CROSS-SECTIONS, CYTOCHROME-C, EGG-WHITE LYSOZYME, H/D EXCHANGE, HYDROGEN-DEUTERIUM EXCHANGE, HYDROGEN/DEUTERIUM EXCHANGE, IONIZATION MASS-SPECTROMETRY, IONS, OF-FLIGHT SYSTEM, PROTEIN, UNFOLDING DYNAMICS},
	isbn = {0003-2700},
	url = {<Go to ISI>://000181675900014},
	author = {Mao, D. M. and Babu, K. R. and Chen, Y. L. and Douglas, D. J.}
}
@article {682,
	title = {H/D exchange of gas phase bradykinin ions in a linear quadrupole ion trap},
	journal = {Journal of the American Society for Mass Spectrometry},
	volume = {14},
	number = {2},
	year = {2003},
	note = {ISI Document Delivery No.: 643ZYTimes Cited: 14Cited Reference Count: 51},
	month = {Feb},
	pages = {85-94},
	type = {Article},
	abstract = {The gas phase H/D exchange reaction of bradykinin ions, as well as fragment ions of bradykinin generated through collisions in an orifice skimmer region, have been studied with a linear quadrupole ion trap (LIT) reflectron time-of-flight (rTOF) mass spectrometer system. The reaction in the trap takes only tens of seconds at a pressure of few mTorr of D2O or CD3OD. The exchange rate and hydrogen exchange level are not sensitive to the trapping q value over a broad range, provided q is not close to the stability boundary (q = 0.908). The relative rates and hydrogen exchange levels of protonated and sodiated +1 and +2 ions are similar to those observed previously by others with a Fourier transform ion cyclotron resonance (FTICR) mass spectrometer system. The doubly and triply protonated ions show multimodal isotopic distributions, suggesting the presence of several different conformations. The y fragment ions show greater exchange rates and levels than a or b ions, and when water or ammonia is lost from the fragment ions, no exchange is observed. (J Am Soc Mass Spectrom 2003, 14, 85-94) (C) 2003 American Society for Mass Spectrometry.},
	keywords = {ACTIVATED DISSOCIATION, COLLISIONAL ACTIVATION, CYTOCHROME-C, HYDROGEN-DEUTERIUM EXCHANGE, HYDROGEN/DEUTERIUM EXCHANGE, INFRARED, IONIZATION MASS-SPECTROMETRY, OF-FLIGHT SYSTEM, PEPTIDE IONS, PROTEIN IONS, RADIATIVE DISSOCIATION},
	isbn = {1044-0305},
	url = {<Go to ISI>://000180894500001},
	author = {Mao, D. M. and Douglas, D. J.}
}
@article {498,
	title = {An atmospheric pressure ion lens that improves nebulizer assisted electrospray ion sources},
	journal = {Journal of the American Society for Mass Spectrometry},
	volume = {13},
	number = {8},
	year = {2002},
	note = {ISI Document Delivery No.: 588METimes Cited: 7Cited Reference Count: 27},
	month = {Aug},
	pages = {906-913},
	type = {Article},
	abstract = {An atmospheric pressure ion lens improves the performance and ease of use of a nebulizer assisted electrospray (ion spray) ion source. The lens is comprised of an oblong-shaped stainless steel ring attached to an external high voltage power supply. The lens is located near the tip of the conductive sprayer, and is maintained at a potential less than that of the sprayer. The ion lens improves the shape of the equipotential lines in the vicinity of the sprayer tip. This lens gives approximately a 2-fold reduction in the signal RSD, a 2-fold increase in the ion signal, an increase in the number of multiply charged ions, and a much broader range of usable sprayer positions. (C) 2002 American Society for Mass Spectrometry.},
	keywords = {CAPILLARY-ZONE-ELECTROPHORESIS, DISSOCIATION, EVAPORATION, IDENTIFICATION, INDUCED, INTERFACE, IONIZATION MASS-SPECTROMETRY, JUNCTION, MECHANISM, PROTEIN-ANALYSIS, SHEATHLESS},
	isbn = {1044-0305},
	url = {<Go to ISI>://000177704600002},
	author = {Schneider, B. B. and Douglas, D. J. and Chen, D. D. Y.}
}
@article {5189,
	title = {Collision-induced dissociation of bradykinin ions in the interface region of an ESI-MS},
	journal = {Journal of the American Society for Mass Spectrometry},
	volume = {12},
	number = {7},
	year = {2001},
	note = {ISI Document Delivery No.: 447HHTimes Cited: 17Cited Reference Count: 42},
	month = {Jul},
	pages = {772-779},
	type = {Article},
	abstract = {By applying different electric field strengths to the orifice-skimmer region of an electrospray ionization mass spectrometer, the rate of dissociation can be varied based on the amount of infernal energy acquired by an ion through collisions: with the curtain gas molecules. Both the Arrhenius equation and Rice-Ramsperger-Kassel (RRK) theory can be used to predict the rate of dissociation of internally excited molecules. A previously determined model for collision-induced dissociation is tested by comparison of predicted and experimentally observed orifice-skimmer potential differences for dissociation of ions. The rate of collision-induced dissociation of bradykinin ions is determined by monitoring the fragments produced in a mass spectrometer. The semi-quantitative model is found to yield effective predictions when accurate Arrhenius and RRK parameters are utilized. (C) 2001 American Society for Mass Spectrometry.},
	keywords = {ACTIVATION, CYTOCHROME-C, ELECTROSPRAY-IONIZATION, GAS-PHASE, IDENTIFICATION, INFRARED RADIATIVE DISSOCIATION, IONIZATION MASS-SPECTROMETRY, MOLECULES, PEPTIDES, PROTEIN IONS},
	isbn = {1044-0305},
	url = {<Go to ISI>://000169565500002},
	author = {Schneider, B. B. and Douglas, D. J. and Chen, D. D. Y.}
}
@article {4726,
	title = {Methanol-induced conformations of myoglobin at pH 4.0},
	journal = {Biochemistry},
	volume = {39},
	number = {47},
	year = {2000},
	note = {ISI Document Delivery No.: 378UETimes Cited: 62Cited Reference Count: 78},
	month = {Nov},
	pages = {14702-14710},
	type = {Article},
	abstract = {The equilibrium methanol-induced conformation changes of holomyoglobin (hMb) at pH 4.0 have been studied by circular dichroism, tryptophan fluorescence, and Soret band absorption and by electrospray ionization mass spectrometry (ESI-MS). Optical spectra show the following: (1) In 35-40\% (v/v) methanol/water, the native-like secondary structure remains, the tertiary structure is lost, the heme protein interactions are decreased, and a folding intermediate is formed. (2) In 50\% methanol, heme is lost from the protein, and there is a small decrease in helicity together with a loss of tertiary structure. (3) At > 60\% methanol, the helicity increases and the apoprotein goes into a helical denatured state. The conformations are also probed by the charge states produced in ESI-MS and by hydrogen/deuterium (H/D) exchange with mass measurement by ESI-MS. At 0-30\% methanol, native hMb produces relatively low charge states (9(+)-13(+)) in ESI-MS and exchanges relatively few hydrogens. In 35-40\% methanol, at which an intermediate is formed, there is a bimodal distribution of hMb ions with both low (9(+)-13(+)) and high (14(+)-23(+)) charge states and also a high charge state distribution (12(+)-26(+)) of apomyoglobin (aMb) ions. Low and high charge states of hMb and a high charge state of aMb all show the same H/D exchange rate, indicating that an unfolded hMb intermediate interconverts between folded hMb and unfolded aMb. The charge state distribution for the unfolded hMb intermediate observed here is similar to that of the recently reported transient intermediate formed during the acid denaturation of hMb. At 50\% alcohol the protein produces predominantly high charge states of aMb ions and shows H/D exchange rates close to those of the acid-denatured protein. H/D exchange of the helical denatured protein at alcohol concentrations >60\%, at which high charge states of aMb are produced, shows that the protein structure is more protected than at similar to 50\% methanol.},
	keywords = {AMIDE HYDROGEN-EXCHANGE, APOMYOGLOBIN, BETA-LACTOGLOBULIN, CYTOCHROME-C, ELECTROSPRAY-IONIZATION, FOLDING INTERMEDIATE, IONIZATION MASS-SPECTROMETRY, MOLTEN GLOBULE INTERMEDIATE, SPERM-WHALE, STRUCTURAL-CHARACTERIZATION, X-RAY-SCATTERING},
	isbn = {0006-2960},
	url = {<Go to ISI>://000165602400040},
	author = {Babu, K. R. and Douglas, D. J.}
}
@article {4305,
	title = {Optimization and immunological characterization of a photochemically coupled lysergic acid diethylamide (LSD) immunogen},
	journal = {Bioconjugate Chemistry},
	volume = {9},
	number = {5},
	year = {1998},
	note = {ISI Document Delivery No.: 125MYTimes Cited: 2Cited Reference Count: 41},
	month = {Sep-Oct},
	pages = {596-603},
	type = {Article},
	abstract = {A photoreactive heterobifunctional linker was used to prepare an immunogen in which lysergic acid diethylamide was indirectly coupled to keyhole limpet hemocyanin at multiple sites on the drug. It was possible to attach approximately 35 drug molecules to each protein using approximately equal amounts of both species during the reaction. The presence of buffer components or water severely compromised reaction efficiency, as estimated from the molar substitution ratio. Factors such as excess linker, pH, irradiation of dry matrix in the absence of buffer, and the drug/protein ratio used during photolysis were shown to have pronounced effects on reaction efficiency. Structural insights regarding immunogen coupling were obtained by determining the specificities of antibodies which were raised against the immunogen. Cross-reactivity data indicated that haptenation of protein likely occurred at positions N1 and N6 of lysergic acid diethylamide, which is plausible given the electrophilicity of the photogenerated aryl nitrene.},
	keywords = {BINDING, CROSS-LINKING REAGENTS, EPITOPE, FUNCTIONALIZED PERFLUOROPHENYL AZIDES, IMMUNOASSAY, IONIZATION MASS-SPECTROMETRY, photolysis, PROTEIN, RADIOIMMUNOASSAY, SERUM-ALBUMIN},
	isbn = {1043-1802},
	url = {<Go to ISI>://000076242400008},
	author = {Kerrigan, S. and Brooks, D. E.}
}
@article {4227,
	title = {Stability of a highly charged noncovalent complex in the gas phase: Holomyoglobin},
	journal = {Rapid Communications in Mass Spectrometry},
	volume = {12},
	number = {15},
	year = {1998},
	note = {ISI Document Delivery No.: 105GATimes Cited: 33Cited Reference Count: 56},
	pages = {1003-1010},
	type = {Article},
	abstract = {Gas phase holomyoglobin (hMb) ions in charge states +7 to +21 were formed by electrospray ionization in combination with a continuous-flow mixing apparatus. Collision cross section measurements show that the highly charged ions are somewhat unfolded in comparison to low charge states but still retain a considerable degree of folding. A new collision model is presented which calculates the relative energies transferred to complexes in tandem mass spectrometry. Tandem mass spectrometry and ion trapping experiments both show that the energies required to dissociate heme from the highly charged heme-protein complexes in the gas phase are similar to those of low charge states, previously shown in literature ion cyclotron resonance experiments to be 0.7-1.0 eV, These energies are comparable to those of the heme binding energy in solution. The results suggest that even for the highly charged hMb ions which have unfolded somewhat, the heme-protein interactions remain relatively unperturbed. (C) 1998 John Wiley \& Sons, Ltd.},
	keywords = {CONFORMATION, CYTOCHROME-C, ELECTROSPRAY-IONIZATION, ion-molecule, IONIZATION MASS-SPECTROMETRY, METMYOGLOBIN, MYOGLOBIN, PROTEIN IONS, PROTON-TRANSFER REACTIVITY, QUADRUPOLE, reaction},
	isbn = {0951-4198},
	url = {<Go to ISI>://000075063300003},
	author = {Chen, Y. L. and Campbell, J. M. and Collings, B. A. and Konermann, L. and Douglas, D. J.}
}
@article {4076,
	title = {Ion-molecule reactions of halocarbon cations with polycyclic aromatic hydrocarbons in a quadrupole ion trap .1. Differentiation of structural isomers},
	journal = {Journal of Mass Spectrometry},
	volume = {32},
	number = {8},
	year = {1997},
	note = {ISI Document Delivery No.: XQ564Times Cited: 9Cited Reference Count: 26},
	month = {Aug},
	pages = {864-874},
	type = {Article},
	abstract = {Ion-molecule reactions between polycyclic aromatic hydrocarbons (PAHs) and ions (R+) generated from halogenated hydrocarbons (dichloromethane, chloroform, carbon tetrachloride, 1,1-dichloroethane, difluoromethane and 1,1-difluoroethane) in a quadrupole ion trap were used to differentiate a series of structural isomers of PAHs. This differentiation was based on the formation of [M + R](+) and [M + R - HX](+) products (X = Cl, F) between the halocarbon ions (R+) and PAH molecules (M). Halomethanes were found to give rise predominantly to the elimination products [M + R - HX](+), while the haloethanes also yielded significant amounts of the [M + R](+) adducts. Differences in the ionization energies of the PAH isomers seem to be partially responsible for this differentiation process, Collision-induced dissociation experiments also revealed structural differences in the adducts of different PAH isomers. (C) 1997 by John Wiley \& Sons, Ltd.},
	keywords = {DIMETHYL ETHER, ETHER CHEMICAL-IONIZATION, GAS-PHASE, halocarbon ions, ion-molecule, IONIZATION MASS-SPECTROMETRY, isomer differentiation, polycycle aromatic hydrocarbons, quadrupole ion trap, REACTIONS},
	isbn = {1076-5174},
	url = {<Go to ISI>://A1997XQ56400009},
	author = {Mosi, A. A. and Cullen, W. R. and Eigendorf, G. K.}
}
@article {3029,
	title = {MICROMORPHOLOGICAL AND C-13 NMR CHARACTERIZATION OF A HUMIC, LIGNIC, AND HISTIC FOLISOL FROM BRITISH-COLUMBIA},
	journal = {Canadian Journal of Soil Science},
	volume = {74},
	number = {1},
	year = {1994},
	note = {ISI Document Delivery No.: NG042Times Cited: 9Cited Reference Count: 39},
	month = {Feb},
	pages = {1-15},
	type = {Article},
	abstract = {The thick folic (mainly upland forest) materials (> 40 cm of accumulated organic material) that occur in the Coastal Western Hemlock Biogeoclimatic Zone in British Columbia have not been described with regard to the spatial interrelationships of the soil constituents in context with the chemical composition of the different horizons. Micromorphological assessment and solid-state C-13 NMR were used to characterize the accumulated folic materials from a Lignic Folisol (northern Vancouver Island), Histic Folisol (Prince Rupert, BC) and a Humic Folisol (Queen Charlotte Islands, BC). Micromorphology provided information on the spatial relationships of the soil constituents and C-13 NMR provided data on the chemical components of the folic materials. Soil faunal activity, primarily from mites, was the dominant soil-forming process observed in the organic horizons of the Folisols, being especially prominent in the Lignic Folisol with the breakdown of woody materials. Solid state C-13 CPMAS NMR spectra facilitated distinguishing three main types of horizons: (1) Horizons derived from accumulated residues (L, Fr, and Hr) showing higher carbohydrate-like C and O-alkyl C values and lower total aromatics; (2) Horizons with advanced decomposition (Hr2, Oh1, and Hd) which were higher in alkyl C; and (3) Horizons derived from ligneous material (Fw and Hdw) where carbohydrate-like C was less than total aromatic C. Implications for adequate nutrient content and forest growth were inferred from the observed micromorphology and chemical composition of the folic materials.},
	keywords = {C-13 NMR, CHEMICAL-COMPOSITION, DECOMPOSITION, FAUNAL ACTIVITY, FOLISOL, FOREST SOILS, IONIZATION MASS-SPECTROMETRY, IR, LITTER, MICROMORPHOLOGY, NITROGEN, NUCLEAR-MAGNETIC-RESONANCE, ORGANIC-MATTER, SPECTROSCOPY},
	isbn = {0008-4271},
	url = {<Go to ISI>://A1994NG04200001},
	author = {Fox, C. A. and Preston, C. M. and Fyfe, C. A.}
}
