PubMed · 305696
The source did not provide an abstract. Follow the original record for more information.
Explore connections, maps & timelines
E Beck. 1978-03-20. [Traumatic shock].. https://pubmed.ncbi.nlm.nih.gov/305696/
Cite the original work for its findings. Save a collection to share your selection of sources.
KEEP EXPLORING
With an enzyme immunoassay (ELISA) the stability of tumor necrosis factor alpha (TNF-alpha) has been determined in serum and plasma with and without addition of a protease inhibitor (Aprotinin, Trasylol) 24 hours, as well as seven days after blood collection. It has been observed, that after blood collection the concentration of TNF-alpha decreases first and increases again six hours, (+4 degrees C) respectively twelve hours (-20 degrees C) later. Reasons for that might be: The active form of TNF-alpha is a trimer, the presence of TNF-binding proteins, the presence of TNF-antibodies. Furthermore it has been found, that TNF-alpha has the highest stability in plasma at -20 degrees C and -70 degrees C. The addition of Aprotinin had no significant influence on the stability.
Explore the source record for details and available documents.
We have completed a molecular dynamics simulation of protein (bovine pancreatic trypsin inhibitor, BPTI) in solution at high pressure (10 kbar). The structural and energetic effects of the application of high pressure to solvated protein are analyzed by comparing the results of the high-pressure simulation with a corresponding simulation at low pressure. The volume of the simulation cell containing one protein molecule plus 2943 water molecules decreases by 24.7% at high pressure. This corresponds to a compressibility for the protein solution of beta = 1.8 x 10(-2) kbar-1. The compressibility of the protein is estimated to be about one-tenth that of bulk water, while the protein hydration layer water is found to have a greater compressibility as compared to the bulk, especially for water associated with hydrophobic groups. The radius of gyration of BPTI decreases by 2% and there is a one third decrease in the protein backbone atomic fluctuations at high pressure. We have analyzed pressure effects on the hydration energy of the protein. The total hydration energy is slightly (4%) more favorable at high pressure even though the surface accessibility of the protein has decreased by a corresponding amount. Large pressure-induced changes in the structure of the hydration shell are observed. Overall, the solvation shell waters appear more ordered at high pressure; the pressure-induced ordering is greatest for nonpolar surface groups. We do not observe evidence of pressure-induced unfolding of the protein over the 100-ps duration of the high-pressure simulation. This is consistent with the results of high-pressure optical experiments on BPTI.(ABSTRACT TRUNCATED AT 250 WORDS)