High impact information on cgd4_2910

• Cryptosporidium parvum oocysts were studied for the expression of aminopeptidase by using amino acids bound to the synthetic fluorescent substrate 7-amino-4-trifluoromethyl coumarin [1].
• With arginyl-6-amino-2-styrylquinoline as a substrate, aminopeptidase activity was observed in permeabilized oocysts and freshly excysted sporozoites but not on intact oocysts or empty oocyst membranes after excystation [1].
• 1. Reverse transcription-polymerase chain reaction indicated that the gene for AP is expressed during sporulation, but expression is absent or greatly reduced in the sporozoites and merozoites [2].
• The AP activity was inhibited by the AP inhibitors bestatin and 1,6-phenanthroline, but not by serine protease inhibitors [2].
• The AP had specificity for synthetic endopeptidase substrates that contain arginine, alanine, or glycine at the N terminus [2].

Anatomical context of cgd4_2910

• After 1 h of incubation, intact oocysts showed no activity; however, homogenization and solubilization with Triton X-114 followed by phase separation yielded a 22-fold increase in aminopeptidase activity in the detergent fraction [1].

References