Abstract
Protein synthesis is crucial for the survival of a living system, and any derangement of this process can cause large imbalances and deficiencies in humans. The measurement of whole body protein turnover in humans was a significant advance on simple nitrogen balance studies. Until recently, however, the advantages of focusing on the measurement of synthesis at the tissue or specific protein level have been overwhelmed by the difficulties. The advent of powerful new methods of mass spectrometry and stable isotope tracer methodology along with effective purification techniques enabled the measurement of protein synthesis at the tissue (liver, gut and muscle), specific protein fraction (mitochondrial and sarcoplasmic) and individual protein (myosin heavy chain, albumin and fibrinogen) levels in humans. This offers better insight into the underlying mechanisms of protein synthesis in disease and health conditions.
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