Purification and characterization of phytase from rat intestinal mucosa

• Published in: Biochimica et biophysica acta Vol. 1075; no. 1; pp. 75 - 82
• Main Authors: Yang, W J, Matsuda, Y, Sano, S, Masutani, H, Nakagawa, H
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 02.09.1991; Elsevier
• Subjects: 6-Phytase - isolation & purification; 6-Phytase - metabolism; Alkaline phosphatase; Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; Blotting, Western; Electrophoresis, Polyacrylamide Gel; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Glycosylation; Hydrogen-Ion Concentration; Hydrolases; Intestinal Mucosa - enzymology; Intestine; Male; Molecular Sequence Data; Molecular Weight; Peptide Mapping; Phytase; Rats; Rats, Inbred Strains; Zinc - chemistry; Alkaline phosphatase; ALPase; SDS; Intestine; Phytase; PAGE; PNPP; CAPS; Purification; Rat; Enzyme; 3-Phytase; Rodentia; 6-Phytase; Gut; Subunit; Vertebrata; Mammalia; Enzymatic activity; Michaelis constant; N terminal-Sequence; pH; Inhibition; Physicochemical properties

Phytase (myo-inositol hexakisphosphate phosphohydrolase; EC. 3.1.3.8 or 3.1.26) was purified from rat intestinal mucosa. The purified enzyme preparation exhibited two protein bands on SDS-polyacrylamide gel electrophoresis with estimated molecular masses of 70 kDa and 90 kDa. Rabbit antisera prepare...