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• W2001175209 abstract "Conditions for extraction of rat brain soluble and particulate cysteine proteinase inhibitors (CPIs) were compared and an optimal one was selected to isolate low- and high-molecular-weight forms active toward papain or brain cathepsins BL. The different forms were purified by affinity chromatography on alkylated papain, and identified on sodium dodecyl sulfate-polyacrylamide gel electrophoresis gels by use of Schiff's reagent, or by immunoblots using antisera to monomer or polymeric forms of human urinary cystatin c, to a human plasma histidine-rich glycoprotein (HRG), or to rat plasma T-kininogen. In particulates containing nuclei (P1) or synaptosomes (P2) the predominant CPI was an 80-kDa glycoprotein cross-reacting to anti-HRG and shown to be a T-kininogen by treatment with TPCK-trypsin, and subsequent bioassay of the released kinins. The levels found in rat brain were approximately 0.5 nmol/g wet weight. The higher-molecular-weight CPI potently inhibited cathepsin L hydrolysis of Leu-enkephalin at the Gly2Gly3 bond with a Ki 10−10 M. In contrast the low-molecular-weight CPIs were present in postmicrosomal fractions (S3) and cross-reacted with anti-cystatin c, but not with anti-HRG, anti-lysozyme, anti-β protein amyloid peptide, or anti-T-kininogen. The low-molecular-weight forms were present at approximately 1 – 1.5 nmol/g wet weight and resembled “cerebrocystatin” purified previously from rat brain cytosol by M. Kopitar, F. Stern, and N. Marks ((1983) Biochem. Biophys. Res. Commun.112, 1000–1006.)." @default.
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• W2001175209 date "1988-12-01" @default.
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• W2001175209 title "Diversity of rat brain cysteine proteinase inhibitors: Isolation of low-molecular-weight cystatins and a higher-molecular weight T-kininogen-like glycoprotein" @default.
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• W2001175209 doi "https://doi.org/10.1016/0003-9861(88)90050-1" @default.
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