Concanavalin A induced inhibition of 5'-nucleotidase from guinea pig skeletal muscle and bull seminal plasma: a comparative study.
Both purified and membrane-bound 5'-nucleotidases (EC 3.1,3.5) from guinea pig skeletal muscle and bull seminal plasma are inhibited by Concanavalin A (Con A). 5'-Nucleotidase purified from skeletal muscle is inhibited by Con A by an apparent uncompetitive process (K'i = 160 nM), while the lectin inhibits the particulate enzyme by an apparent non-competitive process (Ki = K'i = 50 nM). 5'-Nucleotidase purified from bull seminal plasma is inhibited by Con A by an apparent non-competitive process (K'i = Ki = 270 nM), while the membrane-bound enzyme is subjected to a mixed type inhibition by the lectin (K'i greater than Ki; 30 and 14 nM, respectively). The enzyme purified from skeletal muscle exhibits a significant cooperativity in the interaction with Con A. The inhibition of bull seminal plasma particulate 5'-nucleotidase brought about by Con A is not completely reversed by addition of alpha-methyl-D-mannoside.
D015720:5'-Nucleotidase; D000818:Animals; D002417:Cattle; D003208:Concanavalin A / Q000494:pharmacology*; D006168:Guinea Pigs; D007700:Kinetics; D008297:Male; D009132:Muscles / Q000201:enzymology*; D009708:Nucleotidases / Q000037:antagonists & inhibitors* / Q000302:isolation & purification; D009928:Organ Specificity; D012661:Semen / Q000201:enzymology*; D013045:Species Specificity
D003208:Concanavalin A; D009708:Nucleotidases; D015720:5'-Nucleotidase