Tetrameric hemoglobins are the most widely used systems in studying protein cooperativity. Allosteric effects in hemoglobins arise from the switch between a relaxed (R) state and a tense (T) state occurring upon oxygen release. Here we report the 2.0-A crystal structure of the main hemoglobin component of the Antarctic fish Trematomus newnesi, in a partial hemichrome form. The two alpha-subunit...

Changes in mean arterial pressure were monitored in rats following 50% isovolemic exchange transfusion with solutions of chemically modified hemoglobins. Blood pressure responses fall into three categories: 1) an immediate and sustained increase, 2) an immediate yet transient increase, or 3) no significant change either during or subsequent to exchange transfusion. The reactivities of these hem...

Specific ligation states of hemoglobin are, when crystallized, capable of taking on multiple quaternary structures. The relationship between these structures, captured in crystal lattices, and hemoglobin structure in solution remains uncertain. Wide-angle X-ray solution scattering (WAXS) is a sensitive probe of protein structure in solution that can distinguish among similar structures and has ...

A new turbidimetric method for the direct measurement of the solubility of oxy- and deoxyhemoglobins (Hb) in concentrated phosphate buffer has been established. The principle of the method is the formation of a homogeneous emulsion when hemoglobin is introduced in concentrated phosphate buffer. The solubility of the oxy and deoxy forms of Hb A, Hb S, Hb C, Hb F, and Hb CHarlem (beta 6Glu leads ...

The genome sequence of the Antarctic Gram-negative marine eubacterium Pseudoalteromonas haloplanktis TAC125 is a potential source of useful data on proteins from a cold-adapted microorganism. Identifying the bases of protein adaptation to higher or lower temperatures is important to understand the relationship between structure/function and life history on the Earth. The P. haloplanktis TAC125 ...

The geminate recombination of CO with Hb following dissociation by a 10-ns laser pulse has been studied as a function of pH (9.2 and 7.0 without inositol hexaphosphate and 6.0 with inositol hexaphosphate) and temperature (5-35 degrees C). The hemoglobins studied included adult, Rothschild, rabbit, opossum, and carp. Despite significant differences in their structural and functional properties, ...

Previous work (1, 2) suggested that a relationship might exist between the number of reactive cysteine residues in various mammalian hemoglobins and the body weight of the animal from which the hemoglobin comes. These studies depended on amperometric titration of the deoxygenated hemoglobin with mercuric ions. The number of mercuric ions bound per molecule ranged from 1.29 for elephant hemoglob...

The apparent proportion of column-chromatographically measured glycosylated hemoglobin in erythrocytes from an individual with hemoglobins A, S, and G was only 2.3% because the slow glycosylated variant hemoglobins were retarded in the column. In contrast, the value for glycosylated hemoglobin was 7.8% by a new cellulose acetate electrophoretic method that includes use of dextran sulfate buffer...

Aim: It has been known for a long time that the presence of clinically silent hemoglobin (Hb) variants in blood samples could influence the measurement of glycohemoglobin (HbA1c) since these abnormal hemoglobins might interfere with some methodologies. In the present study we describe the first case of Hb Beckman in Turkey. Material and Methods: The variant was detected during the HbA1c measure...