REACTIVITIES OF THE SULPHYDRYL GROUPS OF DOG HEMOGLOBIN

~ D4cee43cb075d0bf26050127652f3adc.200x200

Dog hemoglobin has four sulphydryl groups at positions olfl (G18) and p93 (F9), all of which are titratable with mercurials. Only two of these, however, react with non-mercurial sulphydryl reagents. Kinetic results indicate that the reacting site might be the p”” (F9). An examination of the environment of the alI1 (G18) shows that this sulphydryl must be unreactive towards...

Download 641.06 kB

KEHINDE OKONJO *, ADETOKUNBO TAIWO, MUYIWA BALOGUN and O.B. EKISOLA

Okonjo Kehinde » Born 1942. Educated King's College, Lagos (1957-63). BSc, PhD (University of Ibadan). Retired Professor of Chemistry, University of Ibadan. Currently Professor of Chemistry, Covenant University. Current research interests: Kinetics and thermodynamics of reactions of reaction of Ellman's reagent with hemoglobin sulphydryl groups. Publications in such high impact journals as the Journal of... view full profile

Other publications by this author (view profile)

Temperature-jump Studies on Hemoglobin: Kinetic Evidence for a Non-quaternary Isomerization Process in

Relaxation amplitude analysis of thiocyanate and formate binding to human

Effect of Organic Phosphates on the Sulfhydryl Reactivities of Oxyhemoglobins A and S*

The uptake of protons by heme-linked ionizable groups on azide binding to methemoglobin

Transition of haemoglobin between two tertiary conformations: Inositol hexakisphosphate increases the transition constant and the affinity of sheep haemoglobin for 5,5′-dithiobis(2-nitrobenzoate)

Transition of hemoglobin between two tertiary conformations: Determination of equilibrium and thermodynamic parameters from the reaction of 5,5′-dithiobis(2-nitrobenzoate) with the CysF9[93]β sulfhydryl group

Transition of hemoglobin between two tertiary conformations: The transition constant differs significantly for the major and minor hemoglobins of the Japanese quail (Cortunix cortunix japonica)

Reversible reaction of 5,5′-dithiobis(2-nitrobenzoate) with the CysF9[93]β sulfhydryl groups of the hemoglobins of the domestic cat: Variation of the equilibrium and reverse rate constants with pH

Reversible reaction of 5,5V-dithiobis(2-nitrobenzoate) with the hemoglobins of the domestic cat: Acetylation of NH3 terminal group of the h chain transforms the complex pH dependence of the forward apparent second order rate constant to a simple form

Subunit iron spin heterogeneity in human aquomethemoglobin A

Tertiary conformational transition in sheep hemoglobins induced by reaction with 5,5´-dithiobis(2-nitrobenzoate) and by binding of inositol hexakisphosphate

Ligand-dependent reactivity of the CysB5[23] b sulfhydryl group of the major haemoglobin of chicken

Role of the Relaxation of the Iron(ll1) Ion Spin States Equilibrium in the Kinetics of Ligand Binding to Methaemoglobin

The Effect of Heme-linked Ionizable Groups on Cyanide Binding to Methemoglobin

A second pathway of activation of the Torpedo acetylcholine receptor channel

Desensitization is a property of the cholinergic binding region of the