Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1989-12-1
pubmed:abstractText
Mild periodate oxidation of certain commercially available crosslinked agarose beads (Sepharose CL-4B and CL-6B) results in the generation of aldehydo groups which were useful for immobilization of amino compounds by reductive amination using pyridine borane. Consumption of periodate ion and production of formaldehyde were only observed with crosslinked Sepharose preparations and were correlated with a binding capacity much greater than that of uncross-linked gels when subjected to the reductive amination reaction. Up to 50 mg (approximately 0.73 mumol) of bovine serum albumin and 30 mumol of glycylglycine were coupled per gram of moist oxidized Sepharose CL-6B. The immobilization reaction was shown to proceed at neutral pH requiring about 12 h for completion and to be relatively insensitive to temperature and pyridine borane concentration. The oxidized gel was shown to be stable for at least 2 months upon storage in 0.1 M acetic acid. This method has proven to be useful for the preparation of a variety of affinity matrices and immobilized enzymes.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0003-2697
pubmed:author
pubmed:issnType
Print
pubmed:volume
180
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
114-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Immobilization of proteins on oxidized crosslinked Sepharose preparations by reductive amination.
pubmed:affiliation
Department of Biology, Johns Hopkins University, Baltimore, Maryland 21218.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.