AI Article Synopsis
- The study shows that blocking the E-amino groups of aspartate aminotransferase (asp-ase) using succinylation improves its resistance to digestion by trypsin, an enzyme found in plasma.
- In an experiment with sheep, plasmapheresis using filters connected to cellulose cartridges containing the modified asp-ase effectively reduced levels of asparagine (asp-NH2) and glutamine (glut-NH2) in the plasma over a 21-hour period.
- Importantly, there was no detectable leakage of the enzyme into the plasma from the solid phase during the procedure, indicating a successful method of removing these amino acids without losing the enzyme's structural integrity.
Article Abstract
Blockage of E-amino groups of asp-ase bound to cellulose by succinylation results in a greatly enhanced resistance against tryptic digestion by "plasma enzymes." Plasmapheresis in sheep by plasma filters connected to asp-ase Cellulose cartridges led to decrease of asp-NH2 and glut-NH2 in plasma over 21 hrs with undetectable enzyme leakage from the solid phase.
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