Oxygen binding properties of erythrocruorin from the clam shrimp, Caenestheria inopinata

Ehud Ilan*, Ezra Daniel

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

1. 1. The oxygen binding properties of purified erythrocruorin preparations from the conchostracan Caenestheria inopinata were studied. 2. 2. In the pH range 3.9-10.9 and at 25°C, the oxygen binding affinity attains a minimal value of P 1 2 7.8mm Hg at pH 6.8. 3. 3. An alkaline Bohr effect (ø = -0.19) at the pH range 7.4-8.4 and a smaller reverse Bohr effect (ø = 0.08) at the pH range 3.9-5.5 were observed. 4. 4. The dependence of the Hill coefficient nH on pH shows two pH regions where the value of nH is pH independent: nH 1.2 at pH ≪ 8.0 and nH {reversed tilde equals} 2 at pH ≥ 10.0.

Original languageEnglish
Pages (from-to)505-508
Number of pages4
JournalComparative Biochemistry and Physiology -- Part A: Physiology
Volume94
Issue number3
DOIs
StatePublished - 1989

Fingerprint

Dive into the research topics of 'Oxygen binding properties of erythrocruorin from the clam shrimp, Caenestheria inopinata'. Together they form a unique fingerprint.

Cite this