Author/Editor		Popović, T; Brzin, J; Kos, J; Lenarčič, B; Machleidt, W; Ritonja, A; Hanada, K; Turk, V
Title		A new purification procedure of human kidney cathepsin H, its properties and kinetic data
Type		članek
Source		Biol Chem Hoppe Seyler
Vol. and No.		Letnik 369, št. Suppl
Publication year		1988
Volume		str. 175-83
Language		eng
Abstract		A purification procedure of cathepsin H from human kidney is presented. It includes gel filtration, ion exchange chromatography, and covalent chromatography on thiol Sepharose as an essential step. Purified cathepsin H emerges in an isoelectric focusing gel at pH 6.1 and 6.3. Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate shows a molecular mass of about 28 kDa. Less than 20 percent of the enzyme preparation can be separated into a heavy (24 kDa) and a light chain (4 kDa) after reduction and gel filtration on Sephacryl S-200. The partial amino-acid sequence of human cathepsin H shows its close similarity to rat cathepsin H. Inhibition constants (Ki) of cathepsins H and B with chicken cystatin, two forms of human stefin A, human stefin B, and two forms of human cystatin C are in the range of 10(-9) to 10(-11)M.
Descriptors		CATHEPSINS KIDNEY AMINO ACID SEQUENCE CATHEPSIN B CATHEPSINS CYSTEINE PROTEINASES ELECTROPHORESIS, POLYACRYLAMIDE GEL ISOELECTRIC FOCUSING KINETICS MOLECULAR SEQUENCE DATA