EC Number   |
General Stability |
Reference |
|---|
   3.4.17.20 | activateds TAFI, TAFI, is unstable and highly sensitive to temperature |
670474 |
| 3.4.17.20 | analysis of stability of recombinant wild-type and chimeric mutant isozymes, the chimeric mutants show increase stability and half-life compared to the wild-type TAFI, overview |
652560 |
| 3.4.17.20 | epsilon-aminocaproic acid, heparin or guanidinoethyl-mercaptosuccinic acid stabilize |
653977 |
| 3.4.17.20 | inactivation of TAFIa is the result of the conformational instability of TAFIa and not a direct result of proteolysis of TAFIa. It is possible that the conformational changes that take place as a result of the conformational instability make the inactivated 35800 Da enzyme form more susceptible to proteolysis. epsilon-Aminocaproic acid stabilizes |
651987 |
| 3.4.17.20 | intrinsic stability of activated TAFI (half-life): 6.8 min (wild-type) |
699871 |
| 3.4.17.20 | proteolytic cleavage at Arg330 and subsequent inactivation can be diminished by the addition of 6-aminohexanoic acid, 5-aminopentanoic acid, 7-aminoheptanoic acid, hippuryl-L-Lys, hippuryl-L-Arg, L-Arg, or L-Lys |
28942 |
| 3.4.17.20 | the activated enzyme TAFIa is highly unstable and less soluble compared to inactive TAFI, which is not due to posttranslational modifications, but to a loss of 80% of the attached glycans and a shift in pI of TAFIa, overview |
667710 |
| 3.4.17.20 | the enzyme is spontaneously inactivated by conformational changes |
668341 |
| 3.4.17.20 | very unstable in gel filtration procedures |
28944 |
