Cited by 1.5k
Max Planck Institute of Biochemistry
Publishes on Advanced Proteomics Techniques and Applications, Mass Spectrometry Techniques and Applications, RNA and protein synthesis mechanisms. 370 papers and 25.5k citations.
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Abstract Stable isotope labelling in combination with mass spectrometry has emerged as a powerful tool to identify and relatively quantify thousands of proteins within complex protein mixtures. Here we describe a novel method, termed isotope‐coded protein label (ICPL), which is capable of high‐throughput quantitative proteome profiling on a global scale. Since ICPL is based on stable isotope tagging at the frequent free amino groups of isolated intact proteins, it is applicable to any protein sample, including extracts from tissues or body fluids, and compatible to all separation methods currently employed in proteome studies. The method showed highly accurate and reproducible quantification of proteins and yielded high sequence coverage, indispensable for the detection of post‐translational modifications and protein isoforms. The efficiency ( e.g. accuracy, dynamic range, sensitivity, speed) of the approach is demonstrated by comparative analysis of two differentially spiked proteomes.
A material which displayed opioid activity in the guinea pig ileum longitudinal muscle-myenteric plexus preparation was extracted from an enzymatic casein digest into chloroform/methanol. The extract was roughly purified by adsorption/desorption procedures using charcoal and Amberlite XAD-2 resin as adsorbents. A high degree of purity was achieved by high-pressure liquid chromatography of the material on muBondapak C18 and mu-Porasil columns and finally by gel filtration chromatography on a Bio-Gel P-2 column. Several pronase-resistant compounds with opioid activity were obtained.