Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1975-10-3
pubmed:abstractText
Routine investigation of ante natal patients revealed a subtle change in the electrophoretic pattern on cellulose acetate of the proposita. Further investigations by isoelectric focussing in polyacrylamide gel suggested the presence of two major haemoglobin components. Using a modified cellulose acetate technique globin chain separation revealed an abnormal beta-chain. Chain separation on a carboxymethyl-cellulose column provided a pure sample of the abnormal beta-chain. After amino-ethylation, tryptic digestion and peptide mapping, amino acid analysis of relevant peptides showed the abnormality in the beta-chain to be a substitution of arginine by serine at the 104 position. The presence of a positively charged residue at this position would appear to be necessary for the stabilization of the haemoglobin central cavity. The replacement by serine in this haemoglobin leads to slightly decreased stability but does not appear to affect the oxygen affinity.
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
195-200
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1975
pubmed:articleTitle
Haemoglobin Camperdown beta104(G6) arginine leads to serine.
pubmed:publicationType
Journal Article