Linked Life Data

18546311

Source:http://linkedlifedata.com/resource/pubmed/id/18546311

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2008-6-11
pubmed:abstractText
A method is described for the immobilization on tritylated agarose or Sepharose columns of a wide spectrum of enzymes, including types useful in contemporary biochemistry/molecular biology, many of which have never before been reported as immobilized. The method involves the formation of noncovalent hydrophobic bonds between the enzymes and trityl groups which are attached to the agarose by means of ether bonds. The immobilization of calf intestinal and E. coli alkaline phosphatases to tritylagarose is reported in detail. Their binding strength, binding capacity, and long-term stability (greater than six months) are described as a function of the salt concentration, pH, buffer type, and degree of agarose substitution. Homologies are noted between tritylagarose-bound and membrane-bound phosphatases. This method compares favorably with other methods, covalent or otherwise, reported to date, in terms of the enzyme immobilization yield (ca. 100%), the mildness of conditions, resulting, in most cases, in the retention of a high degree of activity, the ease and speed of the manipulations, and the long-term stability of the immobilized enzyme. Further, it is noted that highly tritylated and crosslinked Sephadex G10 selectively and mildly removes detergents from enzyme solutions.
pubmed:language
eng
pubmed:journal
pubmed:status
PubMed-not-MEDLINE
pubmed:month
Feb
pubmed:issn
0006-3592
pubmed:author
pubmed:issnType
Print
pubmed:volume
24
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
403-23
pubmed:year
1982
pubmed:articleTitle
Enzyme immobilization on tritylagarose.
pubmed:affiliation
Department of Biology, University of New Brunswick, Fredericton, New Brunswick E3B 6E1, Canada.
pubmed:publicationType
Journal Article