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Biomedical subjects

M E John

Publications and source records attributed to M E John.

7 recordsLinked to original sources
PubMed1979

Nitric oxide induced conformational changes in opossum hemoglobin.

Opossum hemoglobin assumes a T quaternary structure upon NO ligation in the absence of organic phophates at pH 6.7. In addition, stripped opossum hemoglobin exhibits a low oxygen affinity when compared to human hemoglobin and a pH-dependent heme-heme interaction with an n value of 2.14 at pH 7.0 and 2.46 at pH 7.35. These observations indicate that opossum hemoglobin may have a destabilized oxy structure when compared to hemoglobin A due to differences in primary structure. Thus, the strong trans ligand effect of nitric oxide is able to disrupt the proximal histidine-iron bond in the alpha-hemes triggering a conformational transition to the T state. Absence of a distal histidine in the alpha-subunits and, therefore an impaired donor acceptor interaction with the sixth ligand, could contribute to the lack of stability of the R quaternary structure in opossum nitrosylhemoglobin. The reduced oxygen affinity of opossum hemoglobin may be compensated for by other physiological factors such as a reduced phosphate effect.

Amino Acids↗
PubMed1979

Differential effects of pH and inositol hexaphosphate on the spectroscopic properties of the alpha and beta subunits in methemoglobins M Milwaukee and A.

The effect of pH and inositol hexaphosphate on the electron spin resonance spectra of the alpha-hemes (g = 6.0) and the beta-hemes (g = 6.7) has been measured in methemoglobin M Milwaukee and compared with that of methemoglobin A (g = 6.0). The beta-hemes are found to be comparatively insensitive to both effectors while the alpha-hemes behave in a manner similar to the heme groups of methemoglobin A. Binding of inositol hexaphosphate enhances the high spin ESR signal of the alpha-hemes in both methemoglobins. Comparison of the optical properties of methemoglobins A and M Milwaukee over the pH range from 5.0 to 8.1 shows that inositol hexaphosphate has a differential effect on the subunit types in these two methemoglobins. At low pH the spectral changes observed upon inositol hexaphosphate binding arise primarily from the beta-hemes, while at neutral and alkaline pH these changes arise from both subunit types. The beta-heme spectral changes appear to be pH independent while those arising from the alpha-hemes are strongly pH dependent. It is concluded that it is the hydroxymet form of the alpha-hemes which undergoes spectral change upon inositol hexaphosphate binding to the beta-subunits. In methemoglobin A the spin state and paramagnetic susceptibility increase only in the neutral and alkaline pH ranges upon inositol hexaphosphate binding (Gupta, R.K. and Mildvan, R.S. (1975) J. Biol. Chem. 250, 246; Perutz, M.F., Sanders, J.K.M., Chenery, D.H., Noble, R.W., Penelly, R.R., Fung, L.W.-M., Ho, C., Giannini, I., Porschke, D. and Winkler, H. (1978) Biochemistry 17, 3640). Therefore the hydroxymet form of the alpha-hemes which is responsible for the observed spectral changes must also be responsible for these increases in the magnetic properties of methemoglobin A. Inositol hexaphosphate can bind to methemoglobin at alkaline pH if the beta-hemes are in the high spin form.

Chemical Phenomena↗
PubMed1978

Gene diversity of bovid hemoglobins.

Forty-five adult hemoglobin molecular forms which include 22 electrophoretically silent forms were structurally characterized from animal species of nine genera belonging to family Bovidae. Of the 12 different bovid species studied, 11 showed either alpha or beta chain heterogeneity in their hemoglobins while eight species showed heterogeneity for both polypeptide chains. Wherever possible, the genetic basis for hemoglobin phenotypes has been suggested. By construction of a phylogenetic tree for 14 ungulate alpha-globin sequences, the evolutionary origins of duplicated alpha chain genes present in some ungulate species have been located, and the phyletic relationship of Bovids based on the alpha globin data is discussed.

Animals↗
PubMed1977

A new hemoglobin beta chain variant in sheep.

A new hemoglobin beta chain variant referred to as Hb-E is observed in four Indian sheep breeds. Hemoglobin E is electrophoretically and chromatographically undistinguishable from hemoglobin B. However, polypeptide chain separation by urea-polyacrylamide disc gel electrophoresis and urea CM-cellulose chromatography reveals the new beta chain. The betaE chain has a slower anodic mobility than betaB chain at alkaline pH. The adult sheep hemoglobins could be classified into eight categories, namely AA, AB, AE, AC, ABC, BB, BE and EE, according to their sub-unit composition. The occurrence of betaE chain in homozygous condition or in combination with either one of the two allelic beta chains betaA or betaB, indicate that it may be an allelic variant. Gene frequencies of three hemoglobin beta chain alleles observed during the study are as follows: A = 0.192; B= 0.682; E = 0.126.

Alleles↗