Physical properties of gamma-glutamyltransferase in human serum.
Using gel chromatography on Sephacryl S300 we have separated serum gamma-glutamyltransferase into three fractions with estimated relative molecular masses of (a) greater than 1000 000, (b) 250 000-500 000 and (c) about 120 000. Similarly, serum leucine aminopeptidase has been separated into three fractions. We have studied, particularly, the gamma-glutamyltransferase fraction of intermediate relative molecular mass (250 000-500 000) in serum from patients with a number of liver diseases. We have shown, both by polyanion and immuno-precipitation, that it consists significantly of a complex between gamma-glutamyltransferase and high density lipoprotein. The physical properties of this fraction, namely its mass and charge, can be altered by incubating serum with either bile or bile salts.
D000469:Alkaline Phosphatase / Q000097:blood; D000838:Anions; D001647:Bile Acids and Salts; D002462:Cell Membrane / Q000201:enzymology; D011232:Chemical Precipitation; D002850:Chromatography, Gel; D003956:Dialysis; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D005615:Freezing; D006801:Humans; D007106:Immune Sera; D007931:Leucyl Aminopeptidase / Q000097:blood; D008074:Lipoproteins / Q000097:blood; D008099:Liver / Q000201:enzymology; D008107:Liver Diseases / Q000175:diagnosis / Q000201:enzymology*; D008297:Male; D008862:Microsomes, Liver / Q000201:enzymology; D010206:Papain; D011485:Protein Binding; D011489:Protein Denaturation; D005723:gamma-Glutamyltransferase / Q000097:blood*
D000838:Anions; D001647:Bile Acids and Salts; D007106:Immune Sera; D008074:Lipoproteins; D005723:gamma-Glutamyltransferase; D000469:Alkaline Phosphatase; D007931:Leucyl Aminopeptidase; D010206:Papain