Comparing the efficiencies of hydrazide labels in the study of protein carbonylation in human serum albumin.

ABSTRACT: In this work, we establish a methodology for comparing the efficiencies of different hydrazide labels for detecting protein carbonyls. We have chosen acrolein-modified human serum albumin as a model. This system provides a convenient means of reproducibly generating carbonylated protein. Five hydrazide-based labels were tested. Three carry a biotin affinity tag, and the others are simple fatty acid hydrazides. For the biotin-based labels, the yield of the labeling reaction varies considerably, and the most commonly used label, biotin hydrazide, gives the lowest yield. The total tandem mass spectrometry (MS/MS) spectrum counts of modified peptides are similar for all of the biotin-based tags, indicating that factors beyond the labeling efficiency are important in determining the effectivene

SUBMITTER: Ugur Z 

PROVIDER: S-EPMC3577925 | biostudies-literature | 2012 Sep

REPOSITORIES: biostudies-literature