Abstract
Lipoprotein lipase (glycerol ester hydrolase ; EC 3.1.1.3) from Pseudomonas fluorescens was oxidized with N-bromosuccinimide at 37°. One mol of tryptophan residue per mol of enzyme was oxidized, but the enzymatic activity was unaffected. The enzyme was inactivated by photooxidation in the presence of methylene blue, and the inactivation was pH-dependent. In addition, the decrease in the enzymatic activity was accompanied by the loss of a histidine residue. It appears that the histidine residue in involved in the catalytic activity of the enzyme.
