Linked Life Data

15913893

Source:http://linkedlifedata.com/resource/pubmed/id/15913893

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2005-6-13
pubmed:abstractText
Site-directed mutagenesis was used to study the role of histidine residues located in domain I in the neutral-to-basic (N-B) transition of human serum albumin (HSA). Based on a previous study of the N-B transition by means of proton NMR, the following recombinant HSA species were synthesized in the yeast species, Pichia pastoris: H9F, H9S, H39F, H39S, H67F, H67S, H105F, H105S, H128F, H128S, H146F, H146S, and wild type HSA. By monitoring the fluorescent intensity of warfarin bound to the above recombinant human serum albumin species as a function of pH, the mutational effect of individual histidine residues on the N-B transition was examined. While H9, H67, H105, H128 and H146 contribute to the transition significantly, H39 appears to have virtually no contribution to the transition. Based on the X-ray crystallographic structure, it is suggested that electrostatic interactions are the principal factor in determining the histidine pK shifts.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
1724
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
37-48
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Site-directed mutagenesis study of the role of histidine residues in the neutral-to-basic transition of human serum albumin.
pubmed:affiliation
Department of Anatomy, Biochemistry, Physiology and Reproductive Biology, John A. Burns School of Medicine, University of Hawaii, 1960 East-West Road., Honolulu, HI 96822, USA.
pubmed:publicationType
Journal Article