Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2003-4-3
pubmed:abstractText
To investigate the modification of recombinant human augmenter of liver regeneration (rhALR) by the urea in purification processes and the biological activity of rhALR and modified rhALR, the molecular weight of proteins and tryptic peptides were determined by matrix-assisted laser desorption time of flight mass spectrometry (MALDI-TOF-MS), and the biological activity of rhALR and modified rhALR was also observed by in vivo experiments. A 30 kD homodimer of rhALR was purified under denaturing conditions. The molecular weight of rhALR is 30 780 if urea was used to denature the inclusion bodies; when the denaturant was guanidine hydrochloride, the molecular weight of rhALR was 30 087. The results of MALDI-TOF-MS of digested rhALR that have been modified by urea showed that peptides that contained lysyl were 43 larger than the theoretical value. Proteins purified by different processes were all able to promote the survival rate of CCl(4)-intoxicated mice. It could be concluded that cyanate, the cleavage product of urea, could react with the epsilon-amino group of lysyl in rhALR, and the modified rhALR had the same biological activity as natural rhALR.
pubmed:language
chi
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0582-9879
pubmed:author
pubmed:issnType
Print
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
355-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
[Modification of recombinant human augmenter of liver regeneration with urea studied by maldi-tof mass spectrometry].
pubmed:affiliation
PLA Centre of Infectious Diseases, Guangzhou Airforce Hospital, Guangzhou 510620, China. xiangping_kong@hotmail.com
pubmed:publicationType
Journal Article, English Abstract