Gγ and Aγ globin chains separation and quantitation by isoelectric focusing

P. Comi, B. Giglioni, S. Ottolenghi, A. M. Gianni, G. Ricco, U. Mazza, G. Saglio, C. Camaschella, P. G. Pich, E. Gianazza, P. G. Righetti

Research output: Contribution to journalArticle

47 Citations (Scopus)

Abstract

Isoelectric focusing in the presence of Nonidet P-40 splits human chromatographically pure γ globin chains into two bands of isoelectric points 6.95 and 6.85, respectively. The comparison of the relative proportions of the two bands with the ratios between the Gγ and Aγ non allelic chains of human fetal hemoglobin suggests that the band at pI 6.95 corresponds to Gγ and the band at pI 6.85 corresponds to the Aγ chain; the latter is the only band present in a patient with Greek type hereditary persistence of fetal hemoglobin, producing only Aγ chains. Fluorography of electrofocusing-separated radioactive γ globin chains synthesized by thalassemic reticulocytes indicates that the relative Gγ Aγ synthetic ratios are similar to the relative amounts of Gγ and Aγ chains accumulated in the erythrocytes, suggesting that the activities for the Gγ and Aγ mRNAs decay at roughly similar rates.

Original languageEnglish
Pages (from-to)1-8
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume87
Issue number1
DOIs
Publication statusPublished - Mar 15 1979

Fingerprint

Fetal Hemoglobin
Globins
Isoelectric Focusing
Photofluorography
Reticulocytes
RNA Stability
Isoelectric Point
Erythrocytes
Messenger RNA
Nonidet P-40

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Comi, P., Giglioni, B., Ottolenghi, S., Gianni, A. M., Ricco, G., Mazza, U., ... Righetti, P. G. (1979). Gγ and Aγ globin chains separation and quantitation by isoelectric focusing. Biochemical and Biophysical Research Communications, 87(1), 1-8. https://doi.org/10.1016/0006-291X(79)91639-5

Gγ and Aγ globin chains separation and quantitation by isoelectric focusing. / Comi, P.; Giglioni, B.; Ottolenghi, S.; Gianni, A. M.; Ricco, G.; Mazza, U.; Saglio, G.; Camaschella, C.; Pich, P. G.; Gianazza, E.; Righetti, P. G.

In: Biochemical and Biophysical Research Communications, Vol. 87, No. 1, 15.03.1979, p. 1-8.

Research output: Contribution to journalArticle

Comi, P, Giglioni, B, Ottolenghi, S, Gianni, AM, Ricco, G, Mazza, U, Saglio, G, Camaschella, C, Pich, PG, Gianazza, E & Righetti, PG 1979, 'Gγ and Aγ globin chains separation and quantitation by isoelectric focusing', Biochemical and Biophysical Research Communications, vol. 87, no. 1, pp. 1-8. https://doi.org/10.1016/0006-291X(79)91639-5
Comi, P. ; Giglioni, B. ; Ottolenghi, S. ; Gianni, A. M. ; Ricco, G. ; Mazza, U. ; Saglio, G. ; Camaschella, C. ; Pich, P. G. ; Gianazza, E. ; Righetti, P. G. / Gγ and Aγ globin chains separation and quantitation by isoelectric focusing. In: Biochemical and Biophysical Research Communications. 1979 ; Vol. 87, No. 1. pp. 1-8.
@article{7b7fdf2b33114ed29fca61f9aa1c952e,
title = "Gγ and Aγ globin chains separation and quantitation by isoelectric focusing",
abstract = "Isoelectric focusing in the presence of Nonidet P-40 splits human chromatographically pure γ globin chains into two bands of isoelectric points 6.95 and 6.85, respectively. The comparison of the relative proportions of the two bands with the ratios between the Gγ and Aγ non allelic chains of human fetal hemoglobin suggests that the band at pI 6.95 corresponds to Gγ and the band at pI 6.85 corresponds to the Aγ chain; the latter is the only band present in a patient with Greek type hereditary persistence of fetal hemoglobin, producing only Aγ chains. Fluorography of electrofocusing-separated radioactive γ globin chains synthesized by thalassemic reticulocytes indicates that the relative Gγ Aγ synthetic ratios are similar to the relative amounts of Gγ and Aγ chains accumulated in the erythrocytes, suggesting that the activities for the Gγ and Aγ mRNAs decay at roughly similar rates.",
author = "P. Comi and B. Giglioni and S. Ottolenghi and Gianni, {A. M.} and G. Ricco and U. Mazza and G. Saglio and C. Camaschella and Pich, {P. G.} and E. Gianazza and Righetti, {P. G.}",
year = "1979",
month = "3",
day = "15",
doi = "10.1016/0006-291X(79)91639-5",
language = "English",
volume = "87",
pages = "1--8",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "1",

}

TY - JOUR

T1 - Gγ and Aγ globin chains separation and quantitation by isoelectric focusing

AU - Comi, P.

AU - Giglioni, B.

AU - Ottolenghi, S.

AU - Gianni, A. M.

AU - Ricco, G.

AU - Mazza, U.

AU - Saglio, G.

AU - Camaschella, C.

AU - Pich, P. G.

AU - Gianazza, E.

AU - Righetti, P. G.

PY - 1979/3/15

Y1 - 1979/3/15

N2 - Isoelectric focusing in the presence of Nonidet P-40 splits human chromatographically pure γ globin chains into two bands of isoelectric points 6.95 and 6.85, respectively. The comparison of the relative proportions of the two bands with the ratios between the Gγ and Aγ non allelic chains of human fetal hemoglobin suggests that the band at pI 6.95 corresponds to Gγ and the band at pI 6.85 corresponds to the Aγ chain; the latter is the only band present in a patient with Greek type hereditary persistence of fetal hemoglobin, producing only Aγ chains. Fluorography of electrofocusing-separated radioactive γ globin chains synthesized by thalassemic reticulocytes indicates that the relative Gγ Aγ synthetic ratios are similar to the relative amounts of Gγ and Aγ chains accumulated in the erythrocytes, suggesting that the activities for the Gγ and Aγ mRNAs decay at roughly similar rates.

AB - Isoelectric focusing in the presence of Nonidet P-40 splits human chromatographically pure γ globin chains into two bands of isoelectric points 6.95 and 6.85, respectively. The comparison of the relative proportions of the two bands with the ratios between the Gγ and Aγ non allelic chains of human fetal hemoglobin suggests that the band at pI 6.95 corresponds to Gγ and the band at pI 6.85 corresponds to the Aγ chain; the latter is the only band present in a patient with Greek type hereditary persistence of fetal hemoglobin, producing only Aγ chains. Fluorography of electrofocusing-separated radioactive γ globin chains synthesized by thalassemic reticulocytes indicates that the relative Gγ Aγ synthetic ratios are similar to the relative amounts of Gγ and Aγ chains accumulated in the erythrocytes, suggesting that the activities for the Gγ and Aγ mRNAs decay at roughly similar rates.

UR - http://www.scopus.com/inward/record.url?scp=0018790999&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0018790999&partnerID=8YFLogxK

U2 - 10.1016/0006-291X(79)91639-5

DO - 10.1016/0006-291X(79)91639-5

M3 - Article

C2 - 454390

AN - SCOPUS:0018790999

VL - 87

SP - 1

EP - 8

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 1

ER -