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Interaction of proteins with Triton X‐100‐substituted sepharose 4B
Author(s) -
NematGorgani Mohsen,
Karimian Khashayar
Publication year - 1984
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260260602
Subject(s) - glutamate dehydrogenase , sepharose , chemistry , bovine serum albumin , chromatography , adsorption , enzyme , biochemistry , immobilized enzyme , dehydrogenase , albumin , hemeprotein , allosteric regulation , glutamate receptor , organic chemistry , receptor , heme
Interaction of a number of arbitrarily chosen proteins with Triton X‐100‐substituted Sepharose 4B has been investigated. Of the proteins examined, bovine serum albumin, hemoglobin, glutamate dehydrogenase, and pepsin were found immobilized on the adsorbent. Binding of these proteins occurred irrespective of pH and NaCl concentration. Cytochrome c, used as a model protein, was totally immobilized only at low pH. Adsorption of glutamate dehydrogenase and pepsin took place with retention of their catalytic activities. Moreover, glutamate dehydrogenase used as a model allosteric enzyme, was found to retain its native properties upon binding to the adsorbent in the forms of suspension or column. Results are discussed in terms of specific interactions involving the hydrophobic region of Triton X‐100 and the apolar patches or crevices present on the surface of protein molecules. Possible potential of the matrix as a method for preparation of biologically active immobilized proteins and its application in continuous operations are also discussed.