Journal
ANALYTICAL AND BIOANALYTICAL CHEMISTRY
Volume 403, Issue 8, Pages 2397-2402Publisher
SPRINGER HEIDELBERG
DOI: 10.1007/s00216-012-5953-3
Keywords
Protein turnover; Respiratory distress syndrome; Selected reaction monitoring; SRM; Protein kinetics; Protein metabolism
Funding
- National Institutes of Health [R01 HL082747, R01 DK069386]
- Genome Training Grant [T32 HG000035]
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We report a method to measure in vivo turnover of four proteins from sequential tracheal aspirates obtained from human newborn infants with respiratory distress syndrome using targeted proteomics. We detected enrichment for all targeted proteins approximately 3 h from the start of infusion of [5,5,5-H-2(3)] leucine, secretion times that varied from 1.2 to 2.5 h, and half lives that ranged between 10 and 21 h. Complement factor B, a component of the alternative pathway of complement activation, had an approximately twofold-longer half-life than the other three proteins. In addition, the kinetics of mature and carboxy-terminal tryptic peptides from the same protein (surfactant protein B) were not statistically different (p = 0.49).
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