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Updated: Jun 19, 2026

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis
Published on: July 31, 2010
A CRYSTALLOGRAPHIC STUDY OF PURE CARBONMON-OXIDE HEMOGLOBIN
1Laboratory of Physiological Chemistry of the University of Illinois College of Medicine, Chicago.
Abstract:
1. Photomicrographs of crystals of pure carbonmonoxide hemoglobin of the following species are presented; ox, sheep, hog, dog, turkey, rat, horse, chicken and guinea pig. Photomicrographs of the oxyhemoglobin crystals of the following species are also shown: ox, sheep, hog, dog, rat, horse and guinea pig. The crystals were formed from the pure protein by adding a suitable amount of ethyl alcohol and maintaining a temperature of 0 degrees C., or lower. 2. In some species a sufficient difference is shown between the carbonmonoxide hemoglobin and oxyhemoglobin crystals to distinguish these compounds, but the photographs of crystals of carbonmonoxide hemoglobin and oxyhemoglobin of some species, such as guinea pig, show no appreciable difference. 3. Differences between the carbonmonoxide hemoglobins, as well as between the oxyhemoglobins, of the different species studied are indicated. 4. The carbonmonoxide hemoglobin crystals from the bloods studied are species specific in their nature, and, in many cases, can be distinguished from the analogous oxyhemoglobin by crystallographic study.
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