Avtor/Urednik		Popović, T; Brzin, J; Ritonja, A; Svetic, B; Turk, V
Naslov		Rapid affinity chromatographic method for the isolation of human cathepsin H
Tip		članek
Vir		J Chromatogr
Vol. in št.		Letnik 615, št. 2
Leto izdaje		1993
Obseg		str. 243-9
Jezik		eng
Abstrakt		Cathepsin H was purified by a single-step affinity chromatographic method from crude human kidney extract. The affinity medium consisted of low-molecular-mass cysteine proteinase inhibitors from potato tubers (PCPIs) coupled to cyanogen bromide-activated Sepharose. The yield of the method is comparable to that of the classical methods. Isoelectric focusing and sodium dodecyl sulphate polyacrylamide electrophoresis showed high purity of the isolated cathepsin H. N-Terminal sequence analysis revealed that intact single-chain cathepsin H was obtained. Binding of the enzyme to the PCPI-Sepharose showed that a free SH group in the cysteine proteinase is not required for complex formation.
Deskriptorji		CATHEPSINS KIDNEY AMINO ACID SEQUENCE CHROMATOGRAPHY, AFFINITY CHROMATOGRAPHY, HIGH PRESSURE LIQUID CYSTEINE PROTEINASE INHIBITORS ELECTROPHORESIS, POLYACRYLAMIDE GEL ENZYME-LINKED IMMUNOSORBENT ASSAY ISOELECTRIC FOCUSING KINETICS MOLECULAR SEQUENCE DATA SEPHAROSE