Electrophoretic characterization of cationic proteins and peptides of buffalo granulocytes

Polymorphonuclear granulocytes contained both nonoxidant and oxidant microb icidal systems of which former is least characterized more particularly in buffaloes. Accordingly cationic proteins were extracted from buffalo periph eral granulocytes and mainly electrophoretically characterized by using AUP AGE. Out of total 11 bands, 3 bands with Rm of 0.64, 0.71 and 0.83 were for peptides just preceding the lysozyme. The band with Rm of 0.87 corresponde d with reference lysozyme, that is maximum cationicity. The remaining bands with relatively poor cationicity represented myeloperoxidase, lactoferrin. and elastase. The peptides on subjecting to the heating treatment lost the ir distinctiveness in AUPAGE. There was no appreciable effect of obtaining granules at 14, 18, 22 and 27 x 1000 g on AUPAGE pattern of their proteins. This was also not much affected by the age of animals. The peptides on tre ating with trypsin lost their band pattern and implied the presence of eith er arginine or lysine in the peptides. The glycoprotein staining of AUPAGE of acid extracted granular proteins revealed the presence: of only 2 bands of glycoprotein type. The peptides isolated by preparative AUPAGE also cont ained no free-SH; carbohydrate groups and proteinase inhibitor activity.