Purification and characterization of cathepsin L from skeletal muscle of the lizard Agama stellio stellio.
Cathepsin L from skeletal muscle of the lizard Agama stellio stellio was purified to homogeneity by ion-exchange and gel-permeation chromatography. The molecular weight of the cathepsin L is estimated to be 34 kD, and its isoelectric point is 5.5. The cathepsin L has a pH optimum of 6.1, requires a thiol-reducing reagent for activation, and is inhibited by cysteine protease inhibitors. The Km and kcat values for Z-Phe-Arg-MCA as substrate are 1.4 microM and 6.2 sec-1, respectively. This enzyme readily hydrolyzes proteins such as insulin B chain, hemoglobin, and serum albumin.
Al-Jassabi
S
S
Biological Sciences Department, Yarmouk University, Irbid, Jordan. sjassabis@hotmail.com
D000818:Animals; D056668:Cathepsin L; D002403:Cathepsins / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D003546:Cysteine Endopeptidases / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases; D004791:Enzyme Inhibitors / Q000494:pharmacology; D008116:Lizards / Q000502:physiology*; D018482:Muscle, Skeletal / Q000201:enzymology*; D013379:Substrate Specificity
D004791:Enzyme Inhibitors; D002403:Cathepsins; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D056668:Cathepsin L