Intramolecular crosslinking of hemoglobin A by sulfosuccinimidyl suberate

Application of crosslinked protein as a blood substitute

B. N. Manjula, A. S. Acharya

Research output: Contribution to journalArticle

Abstract

Sulfosuccinimidyl esters could be targeted to the residues of ββ cleft of hemoglobin A and the bis-sulfosuccinimidyl esters of aliphatic dicarboxylic acids could serve as the `affinity directed' ββ crosslinkers of HbA. The reactivity of sulfosuccinimidyl esters of tartaric acid and sebacic acid with HbA was also investigated to establish the appropriate length of the alkyl chain optimal for the crosslinking reaction.

Original languageEnglish (US)
JournalArtificial Cells, Blood Substitutes, and Immobilization Biotechnology
Volume22
Issue number5
StatePublished - Nov 1994

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Blood substitutes
Hemoglobin A
Blood Substitutes
Hemoglobin
Crosslinking
Esters
Proteins
Acids
Dicarboxylic Acids
Fatty Acids

ASJC Scopus subject areas

  • Biotechnology
  • Biomedical Engineering
  • Biomaterials
  • Hematology

Cite this

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abstract = "Sulfosuccinimidyl esters could be targeted to the residues of ββ cleft of hemoglobin A and the bis-sulfosuccinimidyl esters of aliphatic dicarboxylic acids could serve as the `affinity directed' ββ crosslinkers of HbA. The reactivity of sulfosuccinimidyl esters of tartaric acid and sebacic acid with HbA was also investigated to establish the appropriate length of the alkyl chain optimal for the crosslinking reaction.",
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AB - Sulfosuccinimidyl esters could be targeted to the residues of ββ cleft of hemoglobin A and the bis-sulfosuccinimidyl esters of aliphatic dicarboxylic acids could serve as the `affinity directed' ββ crosslinkers of HbA. The reactivity of sulfosuccinimidyl esters of tartaric acid and sebacic acid with HbA was also investigated to establish the appropriate length of the alkyl chain optimal for the crosslinking reaction.

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