Postsynthetic deamidation of hemoglobin providence (β 82 Lys → Asn, Asp) and its effect on oxygen transport

S. Charache, J. Fox, P. McCurdy, Haig Kazazian, R. Winslow, P. Hathaway, R. van Beneden, M. Jessop

Research output: Contribution to journalArticle

Abstract

Carriers of hemoglobin Providence have three types of β chain in their hemolysates. The two abnormal chains have asparagine (Providence N, Prov N) or aspartic acid (Providence D) at position β 82, instead of lysine. In vitro, only two β chains are synthesized by reticulocytes of carriers, β(A) and β(provN). In vivo studies showed that the specific activity of Providence N was initially 10 fold higher than that of Providence D; the specific activities of the two labeled hemoglobins were approximately equal 5 wk after injection of isotope. Oxygen affinity of carriers' blood was somewhat increased, but they were not polycythemic. The affinity of the purified hemoglobins Providence was decreased. Addition of 2, 3 diphosphoglycerate had little effect on the affinity of either hemoglobin component, and addition of inositol hexaphosphate produced no change in the affinity of Providence D. These studies demonstrate that Providence N is deamidated to Providence D during the life span of the erythrocyte, and suggest this finding may represent only an easily observed prototype of posttranslational modification of proteins in general. Despite an abnormal P 50 of the blood, oxygen transport is probably normal in carriers of the abnormal hemoglobins.

Original languageEnglish (US)
Pages (from-to)652-658
Number of pages7
JournalJournal of Clinical Investigation
Volume59
Issue number4
StatePublished - 1977
Externally publishedYes

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Viperidae
Hemoglobins
Oxygen
Abnormal Hemoglobins
D-Aspartic Acid
2,3-Diphosphoglycerate
Phytic Acid
Asparagine
Reticulocytes
Post Translational Protein Processing
Isotopes
Lysine
Erythrocytes
Injections
Proteins

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Charache, S., Fox, J., McCurdy, P., Kazazian, H., Winslow, R., Hathaway, P., ... Jessop, M. (1977). Postsynthetic deamidation of hemoglobin providence (β 82 Lys → Asn, Asp) and its effect on oxygen transport. Journal of Clinical Investigation, 59(4), 652-658.

Postsynthetic deamidation of hemoglobin providence (β 82 Lys → Asn, Asp) and its effect on oxygen transport. / Charache, S.; Fox, J.; McCurdy, P.; Kazazian, Haig; Winslow, R.; Hathaway, P.; van Beneden, R.; Jessop, M.

In: Journal of Clinical Investigation, Vol. 59, No. 4, 1977, p. 652-658.

Research output: Contribution to journalArticle

Charache, S, Fox, J, McCurdy, P, Kazazian, H, Winslow, R, Hathaway, P, van Beneden, R & Jessop, M 1977, 'Postsynthetic deamidation of hemoglobin providence (β 82 Lys → Asn, Asp) and its effect on oxygen transport', Journal of Clinical Investigation, vol. 59, no. 4, pp. 652-658.
Charache, S. ; Fox, J. ; McCurdy, P. ; Kazazian, Haig ; Winslow, R. ; Hathaway, P. ; van Beneden, R. ; Jessop, M. / Postsynthetic deamidation of hemoglobin providence (β 82 Lys → Asn, Asp) and its effect on oxygen transport. In: Journal of Clinical Investigation. 1977 ; Vol. 59, No. 4. pp. 652-658.
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abstract = "Carriers of hemoglobin Providence have three types of β chain in their hemolysates. The two abnormal chains have asparagine (Providence N, Prov N) or aspartic acid (Providence D) at position β 82, instead of lysine. In vitro, only two β chains are synthesized by reticulocytes of carriers, β(A) and β(provN). In vivo studies showed that the specific activity of Providence N was initially 10 fold higher than that of Providence D; the specific activities of the two labeled hemoglobins were approximately equal 5 wk after injection of isotope. Oxygen affinity of carriers' blood was somewhat increased, but they were not polycythemic. The affinity of the purified hemoglobins Providence was decreased. Addition of 2, 3 diphosphoglycerate had little effect on the affinity of either hemoglobin component, and addition of inositol hexaphosphate produced no change in the affinity of Providence D. These studies demonstrate that Providence N is deamidated to Providence D during the life span of the erythrocyte, and suggest this finding may represent only an easily observed prototype of posttranslational modification of proteins in general. Despite an abnormal P 50 of the blood, oxygen transport is probably normal in carriers of the abnormal hemoglobins.",
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AU - Charache, S.

AU - Fox, J.

AU - McCurdy, P.

AU - Kazazian, Haig

AU - Winslow, R.

AU - Hathaway, P.

AU - van Beneden, R.

AU - Jessop, M.

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N2 - Carriers of hemoglobin Providence have three types of β chain in their hemolysates. The two abnormal chains have asparagine (Providence N, Prov N) or aspartic acid (Providence D) at position β 82, instead of lysine. In vitro, only two β chains are synthesized by reticulocytes of carriers, β(A) and β(provN). In vivo studies showed that the specific activity of Providence N was initially 10 fold higher than that of Providence D; the specific activities of the two labeled hemoglobins were approximately equal 5 wk after injection of isotope. Oxygen affinity of carriers' blood was somewhat increased, but they were not polycythemic. The affinity of the purified hemoglobins Providence was decreased. Addition of 2, 3 diphosphoglycerate had little effect on the affinity of either hemoglobin component, and addition of inositol hexaphosphate produced no change in the affinity of Providence D. These studies demonstrate that Providence N is deamidated to Providence D during the life span of the erythrocyte, and suggest this finding may represent only an easily observed prototype of posttranslational modification of proteins in general. Despite an abnormal P 50 of the blood, oxygen transport is probably normal in carriers of the abnormal hemoglobins.

AB - Carriers of hemoglobin Providence have three types of β chain in their hemolysates. The two abnormal chains have asparagine (Providence N, Prov N) or aspartic acid (Providence D) at position β 82, instead of lysine. In vitro, only two β chains are synthesized by reticulocytes of carriers, β(A) and β(provN). In vivo studies showed that the specific activity of Providence N was initially 10 fold higher than that of Providence D; the specific activities of the two labeled hemoglobins were approximately equal 5 wk after injection of isotope. Oxygen affinity of carriers' blood was somewhat increased, but they were not polycythemic. The affinity of the purified hemoglobins Providence was decreased. Addition of 2, 3 diphosphoglycerate had little effect on the affinity of either hemoglobin component, and addition of inositol hexaphosphate produced no change in the affinity of Providence D. These studies demonstrate that Providence N is deamidated to Providence D during the life span of the erythrocyte, and suggest this finding may represent only an easily observed prototype of posttranslational modification of proteins in general. Despite an abnormal P 50 of the blood, oxygen transport is probably normal in carriers of the abnormal hemoglobins.

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