𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Determination of iron in heme compounds: II. Hemoglobin and myoglobin

✍ Scribed by Bruce F. Cameron


Publisher
Elsevier Science
Year
1965
Tongue
English
Weight
323 KB
Volume
11
Category
Article
ISSN
0003-2697

No coin nor oath required. For personal study only.

✦ Synopsis


The preceding paper in this series (1) describes a rapid and simple determination of total iron in iron porphyrins. The present work extends this method to apply to the naturally occurring hemoproteins, hemoglobin and myoglobin. This requires a digestion to destroy the protein, and some modification of the assay conditions to prevent destruction of the ferrous o-phenanthroline complex formed.


πŸ“œ SIMILAR VOLUMES


Trans-substitution of the proximal hydro
✍ Doug Barrick πŸ“‚ Article πŸ“… 2000 πŸ› John Wiley and Sons 🌐 English βš– 253 KB πŸ‘ 2 views

The trans-substituted histidine to glycine mutant of sperm whale myoglobin (H93G Mb) is used to study energetics of proximal hydrogen bonding, proximal ligand-heme interactions, and coupling to distal ligand binding. Comparison of mono-and dimethylimidazole structural isomers shows that the hydrogen

Kinetics and mechanisms of substitution
✍ Henrique E. Tomam; Fabio S. Nunes πŸ“‚ Article πŸ“… 1993 πŸ› John Wiley and Sons 🌐 English βš– 374 KB πŸ‘ 1 views

The complex [Fe(imox) (Nmim)~], where imox is a planar bis(iminooxime) macrocyclic ligand and Nmim = N-methyl imidazole, undergoes substitution reactions in the presence of 2,2'bipyridine (bipy), leading to a series of intermediate mixed complexes. The forward and reverse rate constants for the subs