Human Hemoglobins

Identification of human hemoglobins.

IFFERENCES IN THE HEMOGLOBINS of the adult and the newborn have been recognized since 1866 (36). Rapid advances in this field, however, began in 1949, when Pauling and Itano (25) discovered that the hemoglobin of sickle cell disease differs from adult hemoglobin. Since that time, 8 hemoglobins have been identified, hemoglobin C (18) in 1950, hemoglobin D (14) in 1951, hemoglobin E (7, 17) and h...

Structure-function relations of human hemoglobins.

In 1949 Pauling and his associates showed that sickle cell hemoglobin (HbS) belonged to an abnormal molecular species. In 1958 Ingram, who used a two-dimensional system of electrophoresis and chromatography to break down the hemoglobin molecule into a mixture of smaller peptides, defined the molecular defect in HbS by showing that it differed from normal adult hemoglobin by only a single peptid...

Hydrogen Exchange Kinetics of Human Hemoglobins

The hydrogen exchange kinetics of human oxy-, deoxy-, and cyanomethemoglobin have been measured as a function of pH by the tritium tracer method. At 5°C and in phosphate buffer both liganded and unliganded forms of ferrohemoglobin exhibit deviations from the regular pH dependence of exchange that is characteristic of cyanomethemoglobin. In oxyhemoglobin, the deviation from the normal exchange p...

Hemoglobins of early human embryonic development.

Plant hemoglobins

Hbs are ubiquitous proteins in most organisms, including bacteria, protozoans, fungi, plants, and animals (Vinogradov et al., 1993; Bolognesi et al., 1997). The known and predicted roles of Hbs in each organism encompass functions that include the reversible binding of gaseous ligands and the ability to bind other cellular molecules. Link to full text: http://www.plantphysiol.org/cgi/content/fu...