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. Author manuscript; available in PMC: 2013 Apr 25.
Published in final edited form as: Anal Biochem. 2011 Jan 20;412(1):47–55. doi: 10.1016/j.ab.2011.01.021

Table 2.

Calculated kinetic parameters and maximum number of incorporated deuterium into tryptic albumin peptides. The total plateau labeling, the turnover constant and half-life for each peptide were calculated using the best fit to a single exponential rise Equations (data are shown as mean ± se). The algorithm described in the text was used to calculate the best fit for the number of exchangeable hydrogens based on minimum of the sum of squares of error (SSE) differences between the observed and theoretical isotopic distribution.

Peptide sequence and
molecular formula		 Calculated
Total Plateau
labeling (%)		 Observed
Fractional Synthetic
Rate (day−1)		 Half-life (day) Maximum number of
incorporated deuterium
N SSE
TCVADENAENCDK
C57 H93 N18 O27 S2 		64.88 ± 0.13 0.41 ± 0.04 1.70 ± 0.17 24 0.00018
SIHTLFGDK
C46 H73 N12 O14 		22.75 ± 0.94 0.36 ± 0.04 1.96 ± 0.24 9 0.00011
LVQEVTDFAK
C52 H85 N12 O17 		39.41 ± 0.18 0.36 ± 0.03 1.93 ± 0.17 15 0.00016
FPNAEFAEITK
C59 H88 N13 O18 		45.58 ± 0.76 0.38 ± 0.04 1.86 ± 0.2 20 0.00011