Avtor/Urednik		Rozman, Jerica; Stojan, Jure; Kuhelj, Robert; Turk, Vito; Turk, Boris
Naslov		Autocatalytic processing of recombinant human procathepsin B is a bimolecular process
Tip		članek
Vir		Febs Lett
Vol. in št.		Letnik 459, št. 3
Leto izdaje		1999
Obseg		str. 358-62
Jezik		eng
Abstrakt		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.
Deskriptorji		CATHEPSIN B ENZYME PRECURSORS PROTEIN PROCESSING, POST-TRANSLATIONAL CATALYSIS CIRCULAR DICHROISM DEXTRAN SULFATE ELECTROPHORESIS, POLYACRYLAMIDE GEL HYDROGEN-ION CONCENTRATION PROTEIN CONFORMATION RECOMBINANT PROTEINS