On proteolytic activity of subcellular fractions of Chlorella vulgaris strain C 111 IBCE C-19 cell

Abstract

Subcellular particles of Chlorella vulgaris C 111 IBCE C-19 were isolated by differential centrifugation in sucrose density gradient. It was stated for the first time, that these particles can cleave casein, gelatin, fibrinogen and hemoglobin at pH 7.4 and 9.0. Using group-specific proteinase inhibitors, a set of serine-, cysteine- and metalloproteinases was identified in this material. However, the detection of this set of proteolytic enzymes is only possible when several different proteins are used as substrates. In some cases, virtually all of the used arsenal of group-specific proteinase inhibitors proved to be little effective. This suggests that these are proteinases of a different nature than those listed above, which requires further perspective research.