Rat pancreatic phospholipase A2: purification, characterization, and N-terminal amino acid sequence.

摘要: Phospholipase A2 was purified from rat pancreas by heat treatment of the homogenate and sequential use DEAE-Sepharose chromatography, CM-Sepharose reverse-phase high-performance liquid chromatography (HPLC). Prophospholipase not separated phospholipase under conditions used, but it well resolved HPLC. The enzyme homogeneous on sodium dodecyl sulfate-polyacrylamide gel electrophoresis analytical HPLC, its molecular weight estimated to be 14,000. specifically hydrolyzed an acylester bond at sn-2-position phospholipid examined. has a pH optimum in range 9.5 10.5 requires presence Ca2+ (3 mM) deoxycholate (0.1%) for activity. amino acid sequence first 32 residues N-terminal region determined. revealed marked homology with those pancreatic phospholipases man, pig, ox, horse, porcine intestinal reported previously.