Localisation of a particulate luliberin hydrolysing activity in microsomal membranes of guinea pig brain.
A particulate luliberin hydrolysing enzyme has been described for guinea pig brain. Examination of subcellular fractions generated under different conditions indicated that particulate luliberin hydrolysing activity was most closely associated with the microsomal marker, rotenone-insensitive NADH cytochrome C reductase. The results obtained indicate that luliberin hydrolysing activity is not associated with synaptosomal membrane preparations and that such luliberin hydrolysing activity as is observed in synaptosomal membranes is probably the result of contamination by microsomes. The enzyme could be released from microsomes by Triton X-100 treatment and the solubilised enzyme was found to be inhibited by puromycin and sulphydryl reagents but to be unaffected by phosphoramidon, captopril, phenylmethyl sulphonyl fluoride and by chelating agents except 1,10-phenanthroline.
Elmore
M A
MA
Department of Biochemistry, University College, Galway, Ireland.
O'Cuinn
G
G
D000135:Acid Phosphatase / Q000378:metabolism; D000818:Animals; D001921:Brain / Q000201:enzymology*; D002462:Cell Membrane / Q000201:enzymology; D007987:Gonadotropin-Releasing Hormone / Q000378:metabolism*; D006168:Guinea Pigs; D006868:Hydrolysis; D008861:Microsomes / Q000201:enzymology*; D009251:NADPH-Ferrihemoprotein Reductase / Q000378:metabolism*; D012402:Rotenone / Q000494:pharmacology; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism; D013385:Succinate Dehydrogenase / Q000378:metabolism; D013574:Synaptosomes / Q000201:enzymology
D012402:Rotenone; D007987:Gonadotropin-Releasing Hormone; D013385:Succinate Dehydrogenase; D009251:NADPH-Ferrihemoprotein Reductase; D000135:Acid Phosphatase; D000254:Sodium-Potassium-Exchanging ATPase