Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 1
pubmed:dateCreated
2004-7-23
pubmed:abstractText
A rapid and simple chromatographic procedure has been developed for the large-scale purification of therapeutic-grade rHuEPO (recombinant human erythropoietin) from medium-conditioned cell cultures, which includes ion-exchange, hydrophobic-interaction and gel-filtration chromatography. A combination of these well-connected steps results in highly purified rHuEPO (> 99%), as revealed by SDS/PAGE and HPLC analyses, with a total yield of 38%. The specific activity of purified rHuEPO was 160,104 i.u./mg. Immunoblotting studies revealed that the protein possesses native EPO immunity. N-terminal sequencing of rHuEPO shows that the first 15 amino acids coincide with those of native EPO reported previously.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0885-4513
pubmed:author
pubmed:issnType
Print
pubmed:volume
40
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
89-94
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
An improved, inexpensive procedure for the large-scale purification of recombinant human erythropoietin.
pubmed:affiliation
Academy of Life Science, Nanjing Normal University, Nanjing 210094, People's Republic of China. ylhu@jlonline.com
pubmed:publicationType
Journal Article, Comparative Study, Evaluation Studies