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Search Publications by: David M. Bunk (Fed)

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Displaying 1 - 25 of 84

Value Assignment of Reference Material 8404 Almond Flour for Allergen Detection

January 21, 2022
Author(s)
Melissa M. Phillips, David M. Bunk, Ashley Beasley Green, James H. Yen
The National Institute of Standards and Technology (NIST) recently released RM 8404 Almond Flour for Allergen Detection, which is intended for harmonizing measurements of allergenic proteins in foods. The material was purchased from a commercial vendor and

Value Assignment of Reference Material 8405 Hazelnut Flour for Allergen Detection

January 21, 2022
Author(s)
Melissa M. Phillips, David M. Bunk, Ashley Beasley Green, James H. Yen
The National Institute of Standards and Technology (NIST) recently released RM 8405 Hazelnut Flour for Allergen Detection, which is intended for harmonizing measurements of allergenic proteins in foods. The material was purchased from a commercial vendor

Feasibility Study of the Use of Frozen Human Sera in Split-Sample Comparison of Immunoassays With Reference Measurement Procedures for Total Thyroxine and Total Triiodothyronine Measurement

October 12, 2021
Author(s)
Linda M. Thienpont, Katleen Van Uytfanghe, J Marriot, Y Tokura, Lothar Siekmann, Anja Kessler, David M. Bunk, Susan Tai
Background: Diagnostic manufacturers must ensure/document metrologically traceable assays. Here we report on a feasibility study that investigated the use of a split-sample comparison with processed, frozen single-donation sera assigned with target values

Reagentless Cleavage of the Peptide Backbone Using Light-Generated Radicals

October 12, 2021
Author(s)
Barbara J. Jones, Mathew J. Vergne, David M. Bunk, Laurie E. Locascio, M A. Hayes
A key step for protein identification and characterization is cleavage into distinct fragments. All current cleavage methods require the addition of reagents, either proteolytic enzymes or chemical agents, and often a second reagent to discontinue cleavage

Harnessing Measurement Science to Advance Food Safety

April 15, 2020
Author(s)
Melissa M. Phillips, David M. Bunk, Carlos A. Gonzalez, Scott A. Jackson, Leah R. Kauffman, Katrice A. Lippa, Catherine A. Rimmer, Stephen Semancik, Michael R. Winchester, Laura J. Wood

Multiplexed LC-MS/MS Assay for Urine Albumin

July 24, 2014
Author(s)
Ashley B. Green, David M. Bunk, Karen W. Phinney
Targeted Multiplexed Assay for Urinary Albumin Quantification Ashley Beasley-Green, Nijah M. Burris, David Bunk, Karen Phinney Biomolecular Measurement Division National Institute of Standards and Technology, Gaithersburg, MD ABSTRACT Urinary excretion of

CPTAC Studies 1 and 5: dissecting variability in multi-site LC-MS/MS proteomics through quality metrics and robust hierarchical multivariate statistics

February 4, 2014
Author(s)
Stephen E. Stein, David M. Bunk, Xia Wang, Matthew Chambers, Lorenzo J. Vega-Montoto, David L. Tabb
Shotgun proteomics experiments integrate a complex sequence of processes, any of which can introduce variability. Quality metrics computed from LC-MS/MS data have relied upon identifying MS/MS scans, but a new mode for the QuaMeter software produces

A reference system for urinary albumin: current status

May 1, 2013
Author(s)
David M. Bunk, Karen W. Phinney, John C. Lieske, Olga Bondar, W. Greg Miller, Lorin M. Bachmann, Andrew S. Narva, Yoshihisa Itoh, Schimmel Heinz
Background: Increased urinary excretion of albumin reflects kidney damage and is a recognized risk factor for progression of renal and cardiovascular disease. Considerable inter-method differences have been reported for both albumin and creatinine

Expression and characterization of 15N-labeled human C-reactive protein in Escherichia coli and Pichia pastoris for use in isotope-dilution mass spectrometry

September 1, 2012
Author(s)
Eric L. Kilpatrick, Wei-Li Liao, Johanna Camara, Illarion V. Turko, David M. Bunk
Isotope dilution mass spectrometry using stable isotope labeled internal standards is unsurpassed in its ability to quantify analytes with accuracy and low measurement uncertainty. The extension of this technique to proteins relies upon the expression of