Thin-layer isoelectric focusing of hemoglobin variants: Screening and determination of isoelectric points

Giuliani, Alessandro; Marinucci, M; Cappabianca, Maria Pia; Maffi, Donatella; Tentori, L

doi:10.1016/0009-8981(78)90079-7

Cited by 8 publications

(1 citation statement)

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“…Our calculated isoelectric point for Hb S, 7.12, is close but not identical to Pauling's and Itano's value of 7.09 [17], and it is closer than values given by other authors. Values for other abnormal hemoglobins are similar to those published by Cuilani et a1 [15] , and qualitatively similar to those of Basset et al [13].…”

Section: Discuss 1 0 Nsupporting

confidence: 89%

Oxygen affinity and stability of hemoglobin dunn (α6(A4)Asp→Asn): Use of isoelectric focusing in recognition of a new abnormal hemoglobin

et al. 1980

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A new slow-moving hemoglobin was found in low proportion in an asymptomatic black woman. Isoelectric focusing helped to distinguish it from other hemoglobins with similar electrophoretic mobility, and amino acid analysis showed that aspartic acid alpha 6 (A4) had been replaced by asparagine. Oxygen affinity was increased, but the Bohr and DPG effects were normal. Stability of the purified hemoglobin was decreased, but that of hemolysates was normal. Abnormal oxygen affinity of this variant, and that of hemoglobin Sawara (alpha 6(A4)Asp replaced by Ala), may reflect loss of a salt bridge between Asp alpha 6 and Lys-alpha 127(H10) which would tend to favor the high-affinity R conformation of the molecule.

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Section: Discuss 1 0 Nsupporting

confidence: 89%