Proteolytic activation of a bovine brain protein with phosphatidylinositol transfer activity

Abstract

We have purified a 38 kDa protein from bovine brain which is cross‐reactive with an affinity purified antibody against the 35 kDa phosphatidylinositol transfer protein from the same source. Controlled trypsinization of the 38 kDa protein yielded an immunoreactive protein of 35 kDa which displayed a 6‐fold increase in phosphatidylinositol transfer activity and a 10‐fold higher affinity for this phospholipid. The possibility that the 38 kDa protein is a precursor of the phosphatidylinositol transfer protein is discussed.