Animals were treated either locally on the site of the anastomosis by a bath of 1 ml of NaBPC157 (2 g/ml or 2 ng/ml), intragastrically or intraperitoneally (10 g or 10 ng/kg b.w.) immediately after anastomosis formation
In 1995, the same group reported structural characterization of a prototypical IDP, prothymosin , using SLS and DLS in combination with SAXS, circular dichroism, and mass spectrometry, indicating that the protein is a biologically active protein with random coil conformation characterized by the shape factor of 1.55 and complete lack of ordered secondary structure and concluding: The finding that a biologically active protein molecule with 109 amino acid residues adopts a random coil conformation under physiological conditions raises the question whether this is a rare or a hitherto-overlooked but widespread phenomenon in the field of macromolecular polypeptides (Gast et al., 1995)
Even though theyre physiologic, theyre less effects
Plastic and Reconstructive Surgery , 121(4), 14211429
Published online 2015 Oct 25