Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1975-10-3
pubmed:abstractText
The characterization of haemoglobin Saki alpha 2 beta 2 14 Leu-Pro(a11) is described. This new mutation is unique since it only induces modification of the stability of the molecule. In vitro precipitation of haemoglobin Saki upon heat or in the presence of chemicals is compared to the stability of haemoglobin A and haemoglobin S.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
393
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
182-7
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:237566-Adult, pubmed-meshheading:237566-Amino Acid Sequence, pubmed-meshheading:237566-Amino Acids, pubmed-meshheading:237566-Diphosphoglyceric Acids, pubmed-meshheading:237566-Drug Stability, pubmed-meshheading:237566-Female, pubmed-meshheading:237566-France, pubmed-meshheading:237566-Hemoglobins, Abnormal, pubmed-meshheading:237566-Hot Temperature, pubmed-meshheading:237566-Humans, pubmed-meshheading:237566-Hydrogen-Ion Concentration, pubmed-meshheading:237566-Isoelectric Focusing, pubmed-meshheading:237566-Japan, pubmed-meshheading:237566-Kinetics, pubmed-meshheading:237566-Leucine, pubmed-meshheading:237566-Oxygen, pubmed-meshheading:237566-Peptide Fragments, pubmed-meshheading:237566-Proline, pubmed-meshheading:237566-Protein Binding, pubmed-meshheading:237566-Time Factors, pubmed-meshheading:237566-Trypsin
pubmed:year
1975
pubmed:articleTitle
Haemoglobin Saki alpha 2 beta 2 14 Leu-Pro(a11) structure and function.
pubmed:publicationType
Journal Article