In this study, the optical properties of glycated (HbA1c) and non-glycated (Hb) hemoglobin are compared using Surface-enhanced Raman spectroscopy (SERS), spectrofluorimetry, refractometry. Analysis spectral shift SERS spectra showed good discrimination between two hemoglobins indicating differences in their molecular structure. The fluorescence measured at excitation wavelengths 260, 270, 280 n...

D URING NORMAL MURINE embryogenesis, erythropoiesis first occurs in the yolk sac blood islands, beginning on days 7-8 of gestation.’ These nucleated erythrocytes primarily synthesize embryonic hemoglobins El (x2y2), Eli (a2y2), and Elil (a2z,).2 5 By day I I of gestation, the fetal liven becomes the major site of red blood cell production, which persists until near birth.6 It has been generally...

Fourth instar larvae of Chironomus thummi were permitted to incorporate labeled amino acids and/or sigma-aminolevulinic acid (sigma-ALA) in vivo and in organ culture. The products secreted into the hemolymph or into the culture medium were examined by acrylamide gel electrophoresis. Nine electrophoretic bands can be resolved as hemoglobins without staining. When gels are sliced for scintillatio...

The heme prosthetic group in hemoglobins is most often attached to the globin through coordination of either one or two histidine side chains. Those proteins with one histidine coordinating the heme iron are called "pentacoordinate" hemoglobins, a group represented by red blood cell hemoglobin and most other oxygen transporters. Those with two histidines are called "hexacoordinate hemoglobins",...

Patients with thalassemia may have abnormal alterations in the proportions of the structurally normal hemoglobins F and A2, or, in more rare circumstances, new hemoglobins of abnormal structure may appear. Such abnormal hemoglobins have not been shown to have substitutions of single amino acids in the polypeptide chain, as exemplified by hemoglobins S and C. Rather, they occur as unusual combin...

Differentiating cells can be characterized by the number and types of proteins they produce (Markert, 1963). In man and other organisms the diversity of hemoglobins has been correlated with ontogenetic changes which reflect the alterations of gene activity (Ingram, 1963). Furthermore, the types of proteins produced are generally specific for the species. The study of insect coelomic proteins ha...

The polypeptide chain composition and the chemical properties of several annelid hemoglobins and chlorocruorins are presented. In agreement with earlier studies on the hemoglobin from Arenicola cristata (Waxman, L. (1971) J. Biol. Chem. 246, 7318-7327), nearly all of the pigments which have been examined consist of one or more different disulfide-linked polypeptide chains of 13,000 to 16,000 da...

The problem of the molecular evolution of hemoglobin has been studied by comparing agar-gel electrophoresis, ultraviolet absorption spectra and resistance to alkalis in fifteen varieties of hemoglobins ranging from human hemoglobin to fish hemoglobin. The differences observed in the hemoglobins seem to be due to differences in the structures of these hemoglobins.

The development of methods (3,4) for localizing the differences in the primary structure of the human hemoglobins has prompted a study of the differences between the structures of hemoglobins A, S, and G. Knowledge of the structural differences might give new insight into the genetic control of the structure of these hemoglobins (5, 6). The results of this study, which are presented here, indic...

A procedure is described for visualization of cells that had only fetal hemoglobin apnormal and mutant adult hemoglobins in peared as clear ghosts. Analyses of cord human blood smears. After extraction of blood from newborn infants indicate that, blood smears with a concentrated poalthough most erythrocytes contain only Hb tassium phosphate buffer (2.76 M, pH 7.2), F and a few contain only Hb A...