Ulrich Kohnert

TL;DR: Modeling studies show that the covalently bound kringle 2 domain in full-length t-PA could interact with an extended hydrophobic groove in the catalytic domain, thus stabilizing the catalytically active conformation without unmasking the Ile276 amino terminus.

TL;DR: The process and storage stability of LDH and rhG-CSF in the vacuum-dried phenylalanine/arginine glasses was greatly improved at temperatures up to 40 degrees C compared with the unprotected proteins, and these sugar-free amino acid formulations thus are potential stabilizes for proteins.

TL;DR: Comparisons with the structures of other serine proteinases that also possess Lys156, such as trypsin, factor Xa and human urokinase plasminogen activator (uPA), identify a set of secondary interactions which are required for Lys156 to fulfil this activating role.

TL;DR: The structure determination of the catalytic domain of tissue-type plasminogen activator (tPA) suggests that the side chain of Arg174 is flexible, and does not play a major role in the S4 specificity of tPA, but this residue would modulate S3 specificity, and may be exploited to fine tune the specificity and selectivity of t PA substrates and inhibitors.

TL;DR: The presence of Tween in only the reconstitution solution appears to inhibit the transition from dimers to higher order oligomers, and the formulations lyophilized with Tween 20 contain the highest levels of aggregates.