An acid endopeptidase was partially purified from normal human red blood cells by ammonium sulphate precipitation, gel filtration chromatography ion exchange chromatography and HPLC. The enzyme had a molecular mass of around 45-54 KD as measured by SDS·PAGE. The endopeptidase does not belong to serine and metallo protease families and seems to be a cathepsin D-like enzyme.
M KAMRAN AZIM ,ZAFAR H ZAIDI ,
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