Differential solubilization of rabbit liver plasma membrane gamma-glutamyltransferase by proteases and detergents: effect of phenobarbital treatment.
In an attempt to understand the mechanism of gamma-glutamyltransferase transfer from the liver to the plasma, potassium chloride, sodium dodecyl sulfate and proteases (papain and bromelain) were used to solubilize rabbit liver plasma membrane gamma-glutamyltransferase. Potassium chloride solutions solubilized 10-30% of membrane proteins but only 1-3% of membrane gamma-glutamyltransferase activity. However, when sodium dodecyl sulfate is used, even at low concentration (0.1-0.2%, w/v) greater than 90% of membrane gamma-glutamyltransferase activity and about 80% of membrane proteins can be solubilized. Furthermore, we showed that unlike the effect of bile salts on the membrane gamma-glutamyltransferase of phenobarbital-treated animals, the same treatment seems to have no influence on membrane gamma-glutamyltransferase solubilization by proteases. Indeed, the ratios of gamma-glutamyltransferase solubilization by papain or bromelain were the same for liver membranes obtained from control and phenobarbital-treated animals.
D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D003902:Detergents; D008099:Liver / Q000201:enzymology*; D008297:Male; D010447:Peptide Hydrolases; D010634:Phenobarbital / Q000494:pharmacology*; D011189:Potassium Chloride; D011817:Rabbits; D012967:Sodium Dodecyl Sulfate; D012995:Solubility; D005723:gamma-Glutamyltransferase / Q000032:analysis*
D003902:Detergents; D012967:Sodium Dodecyl Sulfate; D011189:Potassium Chloride; D005723:gamma-Glutamyltransferase; D010447:Peptide Hydrolases; D010634:Phenobarbital