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Literature DB >> 4524653

Chemical modifications that inhibit gelation of sickle hemoglobin.

Abstract

Substitution of the N-terminal amino groups with pyridoxal compounds inhibits gelation and increases the solubility of deoxy sickle hemoglobin (Hb S). Pyridoxylation of the alpha chains has considerably more effect than that of the beta chains. The increase in minimum gelling concentration of Hb S that results from modification of the alpha N-termini is the same as that produced by dilution of Hb S with an equal amount of Hb A.

Entities: Chemical Gene

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Year: 1974 PMID： 4524653 PMCID： PMC388258 DOI： 10.1073/pnas.71.4.1504

Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205

23 in total

1. Evaluation of sickle hemoglobin and desickling agents by falling ball viscometry.

Authors: N V Paniker; I Ben-Bassat; E Beutler
Journal: J Lab Clin Med Date: 1972-08

2. Relationship between the oxygen affinity and in vitro sickling propensity of carbamylated sickle erythrocytes.

Authors: D Diederich
Journal: Biochem Biophys Res Commun Date: 1972-02-16 Impact factor: 3.575

3. Ligand-induced conformational dependence of hemoglobin in sickling interactios.

Authors: R M Bookchin; R L Nagel
Journal: J Mol Biol Date: 1971-09-14 Impact factor: 5.469

4. Stereochemistry of cooperative effects in haemoglobin.

Authors: M F Perutz
Journal: Nature Date: 1970-11-21 Impact factor: 49.962

5. Hemoglobin O arab in four negro families and its interaction with hemoglobin S and hemoglobin C.

Authors: P F Milner; C Miller; R Grey; M Seakins; W W DeJong; L N Went
Journal: N Engl J Med Date: 1970-12-24 Impact factor: 91.245

6. The effect of beta 73 Asn on the interactions of sickling hemoglobins.

Authors: R M Bookchin; R L Nagel; H M Ranney
Journal: Biochim Biophys Acta Date: 1970-11-17

7. Reduction of methaemoglobin in haemoglobin samples using gel filtration for continuous removal of reaction products.

Authors: H B Dixon; R McIntosh
Journal: Nature Date: 1967-01-28 Impact factor: 49.962

8. Structure and properties of hemoglobin C-Harlem, a human hemoglobin variant with amino acid substitutions in 2 residues of the beta-polypeptide chain.

Authors: R M Bookchin; R L Nagel; H M Ranney
Journal: J Biol Chem Date: 1967-01-25 Impact factor: 5.157

Chemical modifications that inhibit gelation of sickle hemoglobin.

1. Evaluation of sickle hemoglobin and desickling agents by falling ball viscometry.

2. Relationship between the oxygen affinity and in vitro sickling propensity of carbamylated sickle erythrocytes.

3. Ligand-induced conformational dependence of hemoglobin in sickling interactios.

4. Stereochemistry of cooperative effects in haemoglobin.

5. Hemoglobin O arab in four negro families and its interaction with hemoglobin S and hemoglobin C.

6. The effect of beta 73 Asn on the interactions of sickling hemoglobins.

7. Reduction of methaemoglobin in haemoglobin samples using gel filtration for continuous removal of reaction products.

8. Structure and properties of hemoglobin C-Harlem, a human hemoglobin variant with amino acid substitutions in 2 residues of the beta-polypeptide chain.

9. The effects of cyanate in vitro on red blood cell metabolism and function in sickle cell anemia.

10. Potassium cyanate as an inhibitor of the sickling of erythrocytes in vitro.

1. Pyridoxal phosphate as an antisickling agent in vitro.

2. Alternative aspirins as antisickling agents: acetyl-3,5-dibromosalicylic acid.

3. Effects of glyceraldehyde on the structural and functional properties of sickle erythrocytes.

4. Inhibition of erythrocyte sickling in vitro by pyridoxal.

5. Inhibition of erythrocyte sickling in vitro by DL-glyceraldehyde.