l-Glutamine: d-fructose 6-phosphate amidotransferase in tumors and the liver of tumor-bearing animals

• Published in: Biochimica et Biophysica Acta (BBA) - General Subjects Vol. 237; no. 3; pp. 412 - 421
• Main Authors: Kikuchi, Hisako, Kobayashi, Yoshiko, Tsuiki, Shigeru
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 22.06.1971; Elsevier BV
• Subjects: Animals; Ascitic Fluid; Ascitic Fluid - enzymology; Biochemistry; Brain; Brain - enzymology; Carcinoma, Ehrlich Tumor; Carcinoma, Ehrlich Tumor - enzymology; Carcinoma, Hepatocellular; Carcinoma, Hepatocellular - enzymology; Chemical Precipitation; Chromatography, Gel; Colon; Colon - enzymology; Dialysis; Dithiothreitol; Dithiothreitol - pharmacology; Fructosephosphates; Glucosamine; Glucosephosphates; Glutamine; Glycosaminoglycans; Glycosaminoglycans - blood; Hexoses; Hexoses - blood; Intestines; Intestines - enzymology; Kidney; Kidney - enzymology; Kinetics; Liver; Liver - drug effects; Liver - enzymology; Liver Neoplasms; Lung; Lung - enzymology; Male; Metabolism; Mice; Muscles; Muscles - enzymology; Myocardium; Myocardium - enzymology; Neoplasm; Neoplasm Transplantation; Neoplasms, Experimental; Neoplasms, Experimental - enzymology; Nucleoside Diphosphate Sugars; Organs; Rats; Sarcoma, Yoshida; Sarcoma, Yoshida - enzymology; Spleen; Spleen - enzymology; Stomach; Stomach - enzymology; Transaminases; Transaminases - antagonists & inhibitors; Transaminases - blood; Transplantable Tumors: EHRLICH; Types of Tumors; Uracil Nucleotides
• ISSN: 0304-4165; 0006-3002; 1872-8006
• DOI: 10.1016/0304-4165(71)90258-3

1. 1. l-Glutamine: d-fructose 6-phosphate amidotransferase (EC 2.6.1.16) of rat tissues and rat and mouse tumors was studied in crude extracts prepared in the presence of glucose 6-phosphate of after fractionation of the extracts with ammonium sulfate. 2. 2. In rats bearing Yoshida sarcoma, tumor growth was accompanied by substantial increase both in plasma seromucoid and hepatic amidotransferase activity. In rats bearing AH-130 hepatoma, increase in plasma seromucoid was much less marked and their hepatic amidotransferase activity remained within the control range. 3. 3. Of 11 normal rat tissues studied, liver had by far the greatest amidotransferase activity. However, activities greater than that of liver were found in Yoshida sarcoma, AH-130 and mouse Ehrlich ascites carcinoma. The tumor enzyme was considerably more sensitive to UDP- Nacetylglucosamine inhibition than the liver enzyme. 4. 4. Boiled extracts from tumors but not from liver were found to contain an inhibitor specific for amidotransferase. The inhibitor is dialyzable, insensitive to preincubation with UDP- N-acetylglucosamine 2′-epimerase and appears to have been derived from glucose 6-phosphate used for the extraction of amidotransferase.