Affinity chromatography of porcine pepsin on different types of immobilized 3,5-diiodo- l-tyrosine

• Published in: Journal of Chromatography A Vol. 911; no. 2; pp. 211 - 216
• Main Authors: Arnoštová, H., Kučerová, Z., Tišlerová, I., Trnka, T., Tichá, M.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 16.03.2001; Elsevier
• Subjects: Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; Biotechnology; Chromatography, Affinity - methods; Diiodotyrosine; Diiodotyrosine - chemistry; Enzyme engineering; Enzymes; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Hydrolases; Improved methods for extraction and purification of enzymes; Methods. Procedures. Technologies; Pepsin; Swine; Triazines - chemistry; Enzymes; Pepsin; Diiodotyrosine; Immobilized amino acids; Purification; Enzyme; Pepsin A; Agarose; Pig; Affinity adsorbent; Peptidases; Separation method; Vertebrata; Mammalia; Ultraviolet detector; Affinity chromatography; Animal; Hydrolases; Aspartic endopeptidases; Artiodactyla; Ungulata; Modified material
• ISSN: 0021-9673
• DOI: 10.1016/S0021-9673(00)01255-3

The preparation of affinity sorbents containing immobilized iodinated derivatives of l-tyrosine for the affinity chromatography of porcine pepsin is described. The ligand was coupled either to Sepharose 4B or bead cellulose after the divinylsulfone activation or to Sepharose 4B after the activation with 2,4,6-trichloro-1,3,5-triazine. The highest capacity for porcine pepsin was found in the case of 3,5-diiodo- l-tyrosine coupled to divinylsulfone-activated Sepharose.