Serum Protein Binding of Myoglobin, Hemoglobin and Hematin

Serum protein binding of myoglobin, hemoglobin and hematin.

ECENTLY much attention has been focused on the protein binding of hemoglobin. The hemoglobin binding proteins, collectively called haptoglobin, have been thoroughly studied by several workers.’5 Indentification of these substances has helped to clarify the concept of “renal threshold” for hemoglobin excretion.5’6’9 Subsequently, in an investigation of the difference in “renal threshold” of myog...

Carbon monoxide binding by hemoglobin and myoglobin under photodissociating conditions.

Carbon monoxide binding by myoglobin and hemoglobin has been studied under conditions of constant illumination. For hemoglobin, the homotropic heme-heme interaction (cooperativity) and the heterotropic Bohr effect are invariant with light intensity over a 1000-fold change of c((1/2)). The dissociation constant, measured as c((1/2)), increases linearly with light intensity, indicating that photo...

Hemoglobin and Myoglobin

The tertiary structure of myoglobin is that of a typical water soluble globular protein. Its secondary structure is unusual in that it contains a very high proportion (75%) of α-helical secondary structure. A myoglobin polypeptide is comprised of 8 separate right handed α-helices, designated A through H, that are connected by short non helical regions. Amino acid R-groups packed into the interi...

Hemoglobin binding activity and hemoglobin-binding protein of Prevotella nigrescens

Prevotella nigrescens, lacking siderophores was found to bind to the hemoproteins. The binding was observed also in the envelope which was prepared by sonication of the cell. The binding occurred in the pH-dependent manner; the binding was observed below neutral pHs of the incubation mixtures but only slightly observed in the neutral and alkaline pHs. Furthermore, hemoglobin bound to the envelo...

Heme, Myoglobin, Hemoglobin