[A comparative study of aspartyl and cysteine proteinases and their inhibitors in human B- and T-cell leukemias].
A procedure was developed for simultaneous isolation of aspartyl and cysteine proteinases as well as of the cysteine-proteinase inhibitors. Affinity chromatography using pepstatin-Sepharose enabled one to isolate aspartyl proteinases, while inhibitors of cysteine-proteinases were isolated by affinity chromatography on CM-papain-Sepharose; further purification of the enzymes was carried out using ion exchange chromatography and gel filtration. Partially purified preparations of cathepsin D as well as of cysteine-proteinases and their inhibitors were obtained. Some physicochemical and enzymatic properties of the enzymes and inhibitors obtained were studied.
Gureeva
T A
TA
Golubeva
N V
NV
Lubkova
O N
ON
Lokshina
L A
LA
D016282:Aspartic Acid Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003546:Cysteine Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D007525:Isoelectric Focusing; D015448:Leukemia, B-Cell / Q000201:enzymology*; D015458:Leukemia, T-Cell / Q000201:enzymology*; D011480:Protease Inhibitors / Q000494:pharmacology
D011480:Protease Inhibitors; D003546:Cysteine Endopeptidases; D016282:Aspartic Acid Endopeptidases
Sravnitel'noe izuchenie aspartil'nykh, tsisteinovykh porteinaz i ikh ingibitorov v leĭkoznykh B- i T-limfotsitakh cheloveka.