Role of alpha and beta carboxyl-terminal residues in the kinetics of human oxyhemoglobin dimer assembly.

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Article

Role of alpha and beta carboxyl-terminal residues in the kinetics of human oxyhemoglobin dimer assembly.

The Journal of biological chemistry - 18 Mar 1994

Joshi A A, McDonald M J

Abstract excerpt

Human oxyhemoglobin assembly was evaluated in the Soret region by rapidly mixing normal and carboxypeptidase-digested chains (1-10 x 10(-6) M, heme basis) in 0.1 M Tris-HCl, 0.1 M NaCl, 1 mM EDTA, pH 7.4, at 21.5 degrees C. Rate constants of 1.14 (+/- 0.09) and 2.11 (+/- 0.06) x 10(5) M-1 S-1 wer...

Topics

Amino Acid Sequence
Arginine
Genetic Variation
Glutamates
Glutamic Acid
Heme
Hemoglobin A
Hemoglobins, Abnormal
Histidine
Humans
Hydrogen-Ion Concentration
Kinetics
Macromolecular Substances
Oxyhemoglobins
Point Mutation
Spectrophotometry
Tyrosine
Valine

Source

Open in PubMed

Identifiers

PMID: 7907594

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-7907594-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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