Abstract
AbstractThe complete amino acid sequence of ovine phospholipase A2 (EC 3.1.1.4) has been determined. The enzyme consists of a single polypeptide chain containing 123 amino acids, crosslinked by seven disulfide bridges, with a molecular weight of 13804. The enzyme differs at six positions from phospholipase A2 isolated from bovine pancreas1. Both enzymes show similar affinities for Ca2+ ions and hydrolyze monomeric substrates with comparable efficiency.Using monomolecular surface films as a substrate, the ovine enzyme was shown to be able to hydrolyze lipids at slightly higher surface pressures than the bovine enzyme. Direct‐binding studies showed the higher affinity of the ovine enzyme for micelles of the substrate analogue, n‐hexadecylphosphocholine.We suggest that this increased affinity is attributed to a substitution of Asn122 of the bovine enzyme for a tyrosine residue in its ovine counterpart.
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