Half-life, of protein

A short half-life of proteins is often associated with proline, glutamic acid, serine and threonine-rich regions (so-called PEST-rich regions) [Rechsteiner,... 

Intracellularly, proteins are constantly being synthesized, modified, and after the specific function is over, they are routed for degradation. Major factors that determine the half-life of proteins are the presence of signals that control its degradation... 

In vivo, unbound CVAA is quickly excreted via the renal pathway and cannot be detected in urine samples taken later than 12 h post-exposure. However, the biological half-life of protein adducts is much longer in blood samples taken 10 days post-exposure and treated with BAL, Fidder et al. (2000) were still able to release 10% of the CVAA-BAL concentration found on day 1. Thus, protein adducts of CVAA have an important role in the verification of potential lewisite exposure. 

Carbohydrate-specific hepatic receptor-mediated clearance mechanisms include the asialoglycoprotein, S04-GalNAc and Man receptors [235,236]. The asialoglycoprotein receptor on liver hepatocytes is most significant and accounts for the short circulatory half-life of proteins lacking terminal SA [237]. Reliable quantitative analysis of SA will be an important aspect of quality control for glycoprotein pharmaceuticals. For glycoproteins produced in recombinant S. cerevisiae and insect cells which possess terminal Man or Gn moieties, the Man receptor presumably represents a major clearance mechanism [229]. 

Polyethylene glycol modification prolongs the circulating half-life of proteins. Adapted from [34],... 

Reference Proteins studied Reagents used Temp. (°C.) Approx, half-life of protein (hours)... 

Kontermann RE (2011) Strategies for extended serum half-life of protein therapeutics. Curr Opin Chem Biol 22 868-876... 

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