Advanced search
Publication Cover
Hemoglobin
international journal for hemoglobin research
Volume 9, 1985 - Issue 4
Submit an article Journal homepage
11
Views
7
CrossRef citations to date
0
Altmetric
Original Article

A new Case of Hemoglobin Providence (α2 β2 82 (Ef6) Lys → Asn or Asp) Discovered in a French Caucasian Family. Structural and Functional Studies

J. Bardakjian INSERM U-91, Hôpital Henri Mondor, 94010, CRETEIL, France
,
L. Leclerc INSERM U-27, Hôpital Foch, 92150, SURESNES, France
,
Y. Blouquit INSERM U-91, Hôpital Henri Mondor, 94010, CRETEIL, France
,
O. Oules Laboratoire de Biologie, Hôpital E. Roux, 143012, LE-PUY-EN-VELAY, France
,
D. Rafaillat Laboratoire de Biologie, Hôpital E. Roux, 143012, LE-PUY-EN-VELAY, France
,
N. Arous INSERM U-91, Hôpital Henri Mondor, 94010, CRETEIL, France
,
B. Bohn INSERM U-27, Hôpital Foch, 92150, SURESNES, France
,
C. Poyart INSERM U-27, Hôpital Foch, 92150, SURESNES, France
,
J. Rosa INSERM U-91, Hôpital Henri Mondor, 94010, CRETEIL, France
&
F. Galacteros INSERM U-91, Hôpital Henri Mondor, 94010, CRETEIL, France
 show all
Pages 333-348 | Received 12 Nov 1984, Accepted 23 Apr 1985, Published online: 07 Jul 2009

Citations (7)

Keep up to date with the latest research on this topic with citation updates for this article.

Subscribe to citation updates

Read on this site (4)

G. Ivaldi, V. Scimè-Degani, O. David, M. Baffico, M. Baldi, D. Leone, M. Mazzocco, L. Leone, A. Piga, E. Furlan & G. Ricco. (1997) A New Fast-Moving Variant Causing Erythrocytosis and Mild Hemolysis: HB Gàmbara [β82(EF6)Lys→glu]. Hemoglobin 21:4, pages 345-361.
Read now
Y. Ohba, H. Yamada, S. Takamatsu & K. Lmai. (1996) Hb Tsurumai [β82(EF6)LYS → GLN]: A New Hb Variant with High Oxygen Affinity and Erythrocytosis. Hemoglobin 20:2, pages 141-146.
Read now
H. Tonie Wright & Dan W. Urry. (1991) Nonenzymatic Deamidation of Asparaginyl and Glutaminyl Residues in Protein. Critical Reviews in Biochemistry and Molecular Biology 26:1, pages 1-52.
Read now
C. Lacombe, D. Prome, Y. Blouquit, J. Bardakdjian, N. Arous, A. Mrad, J.-C. Prome & J. Rosa. (1990) New Results of Hemoglobin Variant Structure Determinats by Fast Atom Bombardment Mass Spectrometry. Hemoglobin 14:5, pages 529-548.
Read now

Articles from other publishers (3)

Anthony V Signore, Phillip R Morrison, Colin J Brauner, Angela Fago, Roy E Weber & Kevin L Campbell. (2023) Evolution of an extreme hemoglobin phenotype contributed to the sub-Arctic specialization of extinct Steller’s sea cows. eLife 12.
Crossref
A. Dumoulin, L. Kiger, N. Griffon, C. Vasseur, J. Kister, P. Génin, M.C. Marden, J. Pagnier & C. Poyart. (2008) Two mutations in recombinant Hb β F41(C7)Y, K82 (EF6)D show additive effects in decreasing oxygen affinityxs. Protein Science 5:1, pages 114-120.
Crossref
V. Baudin, A. Dumoulin, C. Poyart & J. Pagnier. (1995) Hémoglobine humaine recombinante de faible affinité pour l'oxygène : effets additionnels de deux mutations. Transfusion Clinique et Biologique 2:6, pages 463-467.
Crossref

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Order Reprints Request Corporate Permissions

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

Request Academic Permissions

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.

Related research

People also read lists articles that other readers of this article have read.

Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.

Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.