Ashchmarin I P, Goilo T A, Goncharova V P, Nechaeva G A, Stepanova I S
Biokhimiia. 1975 Mar-Apr;40(2):331-8.
Cationic proteins of brain lysosomes (LCP), myelin (MCP) and nuclear histone fractions from calf thymus (T) and rat brain (B) are shown to increase at different degree the permeability of brain lysosomes and neutrophiles for acid RNAase, acid phosphatase, catepsin D and beta-galactosidase. According to the effectivity, basic proteins can be listed in the following order: for lysosomes-f2aT, F3B, f3T greater than total histones B, f2bT greater than f2B greater than LCP, MCP greater than flT, flB; for neutriphiles-f3T larger than or equal to total histones B larger than or equal to f3b MCP larger than or equal to f2aT, f2bT greater than f2B greater than LCP greater than flB greater than flT. Fractions f2a and f3 considerably increased the release of acid RNAase from lysosomes in very low concentrations beginning from 0,2 mug/ml, while the release of catepsine and acid phosphatase took place beginning from 5-10 mug/ml. The effect of lysosome and myelin cationic proteins on the release of hydrolases occurred at concentrations ten to hundred times higher.