| Author/Editor | Rozman, Jerica; Stojan, Jure; Kuhelj, Robert; Turk, Vito; Turk, Boris | |
| Title | Autocatalytic processing of recombinant human procathepsin B is a bimolecular process | |
| Type | članek | |
| Source | Febs Lett | |
| Vol. and No. | Letnik 459, št. 3 | |
| Publication year | 1999 | |
| Volume | str. 358-62 | |
| Language | eng | |
| Abstract | Cathepsin B and other lysosomal cysteine proteinases are synthesized as inactive zymogens, which are converted to their mature forms by other proteases or by autocatalytic processing. Procathepsin B autoactivation was shown in vitro at pH 4.5 to be a bimolecular process with K(s) and k(cat) values of 2.1+/-0.9 microM and 0.12+/-0.02 s(-1)6.0. However, in the presence of 0.5 microg/ml of dextran sulfate, relatively rapid processing is observed even at pH 6.5 (t(1/2) approximately 90 min), suggesting that glycosaminoglycans are involved in in vivo processing of lysosomal cysteine proteases. | |
| Descriptors | CATHEPSIN B ENZYME PRECURSORS PROTEIN PROCESSING, POST-TRANSLATIONAL CATALYSIS CIRCULAR DICHROISM DEXTRAN SULFATE ELECTROPHORESIS, POLYACRYLAMIDE GEL HYDROGEN-ION CONCENTRATION PROTEIN CONFORMATION RECOMBINANT PROTEINS |