Proteomic analysis of normal human urinary proteins isolated by acetone precipitation or ultracentrifugation Visith Thongboonkerd, Kenneth R. Mcleish,

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Proteomic analysis of normal human urinary proteins isolated by acetone precipitation or ultracentrifugation Visith Thongboonkerd, Kenneth R. Mcleish, John M. Arthur, Jon B. Klein Kidney International Volume 62, Issue 4, Pages 1461-1469 (October 2002) DOI: 10.1111/j.1523-1755.2002.kid565.x Copyright © 2002 International Society of Nephrology Terms and Conditions

Figure 1 Proteome map of human urine. The urine samples were fractionated by two different methods, acetone precipitation (A) and ultracentrifugation (B). The proteins were separated by 2D-PAGE based on their differential pH value for the isoelectric point (pI; x-axis) and molecular weights (y-axis). The protein spots were excised and underwent in-gel tryptic digestion followed by MALDI-TOF MS. Peptide mass fingerprinting were performed to identify the proteins using the Profound search engine query to the entire NCBI protein database. Only the identities with significant Z scores (greater than 1.65) were included. Number labeling in the figure corresponds to the number in Tables 1 and 2. Kidney International 2002 62, 1461-1469DOI: (10.1111/j.1523-1755.2002.kid565.x) Copyright © 2002 International Society of Nephrology Terms and Conditions

Figure 1 Proteome map of human urine. The urine samples were fractionated by two different methods, acetone precipitation (A) and ultracentrifugation (B). The proteins were separated by 2D-PAGE based on their differential pH value for the isoelectric point (pI; x-axis) and molecular weights (y-axis). The protein spots were excised and underwent in-gel tryptic digestion followed by MALDI-TOF MS. Peptide mass fingerprinting were performed to identify the proteins using the Profound search engine query to the entire NCBI protein database. Only the identities with significant Z scores (greater than 1.65) were included. Number labeling in the figure corresponds to the number in Tables 1 and 2. Kidney International 2002 62, 1461-1469DOI: (10.1111/j.1523-1755.2002.kid565.x) Copyright © 2002 International Society of Nephrology Terms and Conditions

Figure 2 Kyte-Doolittle hydropathy plot. Each amino acid residue had a variable hydropathic index varying from negative (hydrophilic) to positive (hydrophobic). The plot was created from each value of hydropathic index along the amino acid sequence of sodium bicarbonate cotransporter (A) and aminopeptidase M (B) from ultracentrifuged urine, and kininogen precursor (C) and IgG (D) from acetone-precipitated urine. The average hydropathic index was from a summation of the entire residues (-0.025, -0.316, -0.765 and -0.500, respectively). Predicted transmembrane portions of each protein (13, 12, 2, and 1, respectively) were consistent with the hydrophobicity. Kidney International 2002 62, 1461-1469DOI: (10.1111/j.1523-1755.2002.kid565.x) Copyright © 2002 International Society of Nephrology Terms and Conditions

Figure 2 Kyte-Doolittle hydropathy plot. Each amino acid residue had a variable hydropathic index varying from negative (hydrophilic) to positive (hydrophobic). The plot was created from each value of hydropathic index along the amino acid sequence of sodium bicarbonate cotransporter (A) and aminopeptidase M (B) from ultracentrifuged urine, and kininogen precursor (C) and IgG (D) from acetone-precipitated urine. The average hydropathic index was from a summation of the entire residues (-0.025, -0.316, -0.765 and -0.500, respectively). Predicted transmembrane portions of each protein (13, 12, 2, and 1, respectively) were consistent with the hydrophobicity. Kidney International 2002 62, 1461-1469DOI: (10.1111/j.1523-1755.2002.kid565.x) Copyright © 2002 International Society of Nephrology Terms and Conditions