Some physicochemical properties of cathepsin H from human meningioma.
OBJECTIVE
To compare some physicochemical properties of cathepsin H from human brain tumors and normal brain tissues.


METHODS
The enzyme was isolated from normal human brain tissue and fibrous meningioma and purified by methods of homogenization, saturation by (NH(4))(2)SO(4) (30-80% saturation), followed by Concanavalin A and Azocazein-Sepharose chromatographies and gel filtration on Sephadex G-100 (75).


RESULTS
Cathepsin H was purified by 1795-fold from normal human brain tissue and by 2457-fold--from meningioma tissue. V(max) for cathepsin H from meningioma was found to be 3.5 times higher than that of normal brain tissue, whilst K(m) of the enzyme from tumor tissue is 1.3 times lower than that from normal human brain. The molecular weights of cathepsin H from normal human brain tissue and meningioma were 28 kDa and 25 kDa respectively.


CONCLUSIONS
Cathepsin H isolated from human fibrous meningioma with microconcentric structures possesses higher activity levels and V(max) value and lower molecular weight than the enzyme from normal human neocortex tissue, without alteration in its pH optimum and K(m) value.
Chornaya
Valentina
V
Department of Experimental Physics, Dniepropetrovsk National University, Dniepropetrovsk 49050, Ukraine.
Lyannaya
Olga
O
D001344:Autopsy; D001706:Biopsy; D056655:Cathepsin H; D002403:Cathepsins / Q000032:analysis / Q000737:chemistry* / Q000494:pharmacology*; D003546:Cysteine Endopeptidases / Q000032:analysis / Q000737:chemistry* / Q000494:pharmacology*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008577:Meningeal Neoplasms / Q000737:chemistry*; D008579:Meningioma / Q000737:chemistry*
D002403:Cathepsins; D003546:Cysteine Endopeptidases; C534126:CTSH protein, human; D056655:Cathepsin H