Changes of serum alkaline phosphatase isoenzymes in fasted rats

• Published in: Journal of Nutritional Science and Vitaminology Vol. 42; no. 5; pp. 435 - 447
• Main Authors: Wada, H. (Gifu Univ. (Japan)), Niwa, N, Hayakawa, T, Tsuge, H
• Format: Journal Article
• Language: English
• Published: Tokyo Center for Academic Publications Japan 1996
• Subjects: ALKALINE PHOSPHATASE; Alkaline Phosphatase - antagonists & inhibitors; Alkaline Phosphatase - blood; Alkaline Phosphatase - metabolism; Animals; Biological and medical sciences; BLOOD SERUM; Bone and Bones - enzymology; Electrophoresis, Polyacrylamide Gel; Enzyme Inhibitors - pharmacology; fasting; Fasting - physiology; Feeding. Feeding behavior; FOSFATASA ALCALINA; Fundamental and applied biological sciences. Psychology; Homoarginine - pharmacology; INANICION; INANITION; Intestines - enzymology; ISOENZIMAS; ISOENZYME; ISOENZYMES; Isoenzymes - antagonists & inhibitors; Isoenzymes - blood; Isoenzymes - metabolism; Kidney - enzymology; Liver - enzymology; Male; Phenylalanine - pharmacology; PHOSPHATASE ALCALINE; polyacrylamide gel electrophoresis; RAT; RATA; RATS; Rats, Sprague-Dawley; serum alkaline phosphatase; SERUM SANGUIN; STARVATION; SUERO SANGUINEO; Vertebrates: anatomy and physiology, studies on body, several organs or systems; Wheat Germ Agglutinins - pharmacology; Alkaline phosphatase; Fasting; Rat; Enzyme; Gel electrophoresis; Isozyme; Rodentia; Phosphoric monoester hydrolases; Esterases; Feeding; Separation method; Vertebrata; Mammalia; Enzymatic activity; Hydrolases; Serum; Physicochemical properties
• ISSN: 0301-4800; 1881-7742
• DOI: 10.3177/jnsv.42.435

Changes of serum alkaline phosphatase (sALP) isoenzymes under fasting conditions were examined using polyacrylamide gel electrophoresis (PAGE), amino-acids (L-phenylalanine (L-Phe), L-homoarginine (L-HArg)) inhibition and wheat germ agglutinin (WGA) treatment. The sALP of non-fasted rats was separated into three bands (Sl, S2, S3) by PAGE. The molecular weight (M.W.) of S 1 corresponded to that of an isoenzyme found in the ileum. By the addition of L-Phe, the staining intensity of 51 was weakened, S2 and S3 remained unchanged and the total activity of the isoenzymes extracted from intestine decreased. On the other hand, the activity of isoenzymes extracted from kidney and bone decreased by the addition of L-HArg. Therefore, S 1 was judged to be derived from intestine. The activities of total sALP and S 1 decreased from 16 h of fasting. Total sALP activity and sALP activity of the supernatant prepared by WGA treatment decreased, whereas the ALP activity of the precipitate (difference between total sALP activity and supernatant sALP activity) did not change. The activity band of the precipitate corresponded to that of S3 by PAGE. Therefore, 53 was judged to be derived from bone. In conclusion, under fasting conditions, the activity of S1 decreased while the activities of S2 and S3 remained unchanged.