Linked Life Data

24784

Source:http://linkedlifedata.com/resource/pubmed/id/24784

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1978-5-8
pubmed:abstractText
The increasing awareness of the importance of the divalent cation zinc in normal and pathologic cell functions has prompted our investigations into the mechanism and control of human erythrocyte zinc uptake. The albumin in blood plasma appears to be the main zinc binding moiety, effectively limiting zinc availability ot the red cell. In non-protein and non-phosphate-containing buffers (i.e., bicarbonate or Tris buffer) red cells sequester more than 90% of the extracellular zinc within 10--15 minutes at a rate more than 250 times faster than zink uptake by cells in plasma. In an albumin-containing media, the influx on red blood cell zinc is lightly temperature sensitive (decreased) between 37 degrees C and 25 degrees C, whereas with cells in bicarbonate buffer alone temperature sensitivity does not begin until below 25 degrees C. Over the physiological range, pH variation has a minimal effect on zinc uptake regardless of the media employed. Finally, once associated with the red cell zinc tends to remain, with a zinc efflux less than 2% of influx. We conclude that human erythrocytes are highly permeable to zinc, with the rate and amount of zinc taken up controlled primarily by the zinc binding characteristics of the media in which the cells are suspended.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0302-2137
pubmed:author
pubmed:issnType
Print
pubmed:volume
56
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5-10
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1978
pubmed:articleTitle
The mechanism and control of human erythrocyte zinc uptake.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.