A hemolytic protein was purified from cultured mycelia of T. clypeatus. Some of the physico-chemical properties of the hemolysin were studied. The protein was analysed to be a lipoprotein and delipidation removed its hemolytic property. The monomeric protein subunit of the lipoprotein had a molecular weight of 64,000. Mode of action of the hemolysin were studied by observing protections of sugar and lipid components to hemolysin mediated lysis of red blood cells. It was observed that the hemolysin possibly interacted with the phospholipid components of the blood cells causing lysis.