1965
DOI: 10.1136/jmg.2.1.48
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Human Haemoglobins

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Cited by 173 publications
(51 citation statements)
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References 139 publications
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“…The ,8:a ratios in these hemoglobins range from 0.8 to 0.9. For two of these hemoglobins (Hbs Koln and Abraham Lincoln), experimental evidence suggested that this slight imbalance in globin chain synthesis is the result of early degradation of the unstable a-chain (41,46 (31).…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…The ,8:a ratios in these hemoglobins range from 0.8 to 0.9. For two of these hemoglobins (Hbs Koln and Abraham Lincoln), experimental evidence suggested that this slight imbalance in globin chain synthesis is the result of early degradation of the unstable a-chain (41,46 (31).…”
Section: Resultsmentioning
confidence: 99%
“…Because the ,3A:a ratio remained nearly constant in the pulse-chase studies, and no,8A was found in the stroma, it may be concluded that very few ,8A or a-chains become associated with the membrane during the chase. If (40,41), Hammersmith (42), Bristol (43), 45), and Abraham Lincoln (46). The ,8:a ratios in these hemoglobins range from 0.8 to 0.9.…”
Section: Resultsmentioning
confidence: 99%
“…No hemoglobins other than A2, F, and S were detectable by electrophoresis in polyacrylamide gel (7) or starch gel (8) in any patient used in these studies. Electrophoresis of hemoglobin in agar gel at pH 6.2 (9) and solubility studies (10) eliminated the possibility of Hb SD disease.…”
Section: Patientsmentioning
confidence: 99%
“…To locate haem-binding proteins, a small amount of haemolysate was added to the serum samples before electrophoresis in another gel which was stained with o-dianisidine for the peroxidase activity exhibited by haem groups (Owen and Smith 1961). Haemolysates were examined for haemoglobin variation by starch-gel electrophoresis using the buffer system of Smithies (Huehns and Shooter 1965).…”
Section: Methodsmentioning
confidence: 99%