scholarly journals The Electrophoretic and Spectroscopic Characterization of Hgb M

Blood ◽  
1958 ◽  
Vol 13 (10) ◽  
pp. 936-949 ◽  
Author(s):  
PARK S. GERALD
Keyword(s):  
Relative Concentration ◽  
Spectroscopic Characterization ◽  
Spectroscopic Studies ◽  
Spectral Curves ◽  
Spectral Changes ◽  
Electrophoretic Behavior ◽  
Patient Reported ◽  
High Concentrations

Abstract The hemoglobin (hgb) from a patient with Hgb M disease was resolved into two components by starch block electrophoresis (at pH 7.0-7.2) of the oxidized hemolyzate. One component was identified electrophoretically and spectroscopically as Hgb A, and the other as Hgb M. Methods for the determination of the relative concentration of Hgb M were given. In the patient reported, Hgb M was found to comprise approximately 30 per cent of the total hgb. Spectroscopic studies of electrophoreticably isolated Hgb M demonstrated that both the methgb and the cyanmethgb form were abnormal in their spectral curves. The reactions of the methgb form with low and high concentrations of cyanide were found to differ. The nature of the spectral changes were such as to indicate that some of the heme groups of the methgb form react abnormally and others apparently normally. The electrophoretic behavior of the patient’s hemolyzate after treatment with various combinations of cyanide and ferricyanide was consistent with this hypothesis. The differing reactivity of the heme groups was explained in the light of the biochemical genetics of the abnormal hemoglobins.

scholarly journals 4-[(2,4-Dichlorophenyl)carbamoyl]butanoic Acid

Molbank ◽  
10.3390/m1227 ◽  
2021 ◽  
Vol 2021 (2) ◽  
pp. M1227
Author(s):  
Bibi Hanifa ◽  
Muhammad Sirajuddin ◽  
Zafran Ullah ◽  
Sumera Mahboob ◽  
See Mun Lee ◽  
...  
Keyword(s):  
Torsion Angle ◽  
Acid Amide ◽  
Spectroscopic Characterization ◽  
Amide Bond ◽  
Amide Hydrogen ◽  
Butanoic Acid ◽  
X Ray ◽  
Amide Derivative

The synthesis and spectroscopic characterization of the glutaric acid-amide derivative, 2,4-Cl2C6H3N(H)C(=O)(CH2)3C(=O)OH (1), are described. The X-ray crystal structure determination of (1) shows the backbone of the molecule to be kinked about the methylene-C–N(amide) bond as seen in the C(p)–N–C(m)–C(m) torsion angle of −157.0(2)°; m = methylene and p = phenyl. An additional twist in the molecule is noted between the amide and phenyl groups as reflected in the C(m)–N–C(p)–C(p) torsion angle of 138.2(2)°. The most prominent feature of the molecular packing is the formation of supramolecular tapes assembled through carboxylic acid-O–H…O(carbonyl) and amide-N–H…O(amide) hydrogen bonding.

scholarly journals Spectroscopic Characterization of Poly(ortho-Aminophenol) Film Electrodes: A Review Article

2013 ◽  
Vol 2013 ◽  
pp. 1-26 ◽  
Author(s):  
Ricardo Tucceri ◽  
Pablo Maximiliano Arnal ◽  
Alberto Néstor Scian
Keyword(s):  
Spectroscopic Characterization ◽  
Spectroscopic Studies ◽  
Review Article ◽  
Electro Oxidation ◽  
Redox Conversion

This paper refers to spectroscopic studies carried out to identify the products ofo-aminophenol electro-oxidation and elucidate the structure of electrochemically synthesized poly(o-aminophenol) (POAP) films. Spectroscopic studies of the redox conversion of POAP are also reviewed.

scholarly journals Functional, structural, and spectroscopic characterization of a glutathione-ligated [2Fe–2S] cluster in poplar glutaredoxin C1

2007 ◽  
Vol 104 (18) ◽  
pp. 7379-7384 ◽  
Author(s):  
Nicolas Rouhier ◽  
Hideaki Unno ◽  
Sibali Bandyopadhyay ◽  
Lluis Masip ◽  
Sung-Kun Kim ◽  
...  
Keyword(s):  
Intracellular Localization ◽  
Spectroscopic Characterization ◽  
Spectroscopic Studies ◽  
Iron Sulfur Cluster ◽  
X Ray Crystallography ◽  
Iron Sulfur ◽  
Catalytic Cysteine ◽  
A Subunit ◽  
Stress Sensing

When expressed in Escherichia coli, cytosolic poplar glutaredoxin C1 (CGYC active site) exists as a dimeric iron–sulfur-containing holoprotein or as a monomeric apoprotein in solution. Analytical and spectroscopic studies of wild-type protein and site-directed variants and structural characterization of the holoprotein by using x-ray crystallography indicate that the holoprotein contains a subunit-bridging [2Fe–2S] cluster that is ligated by the catalytic cysteines of two glutaredoxins and the cysteines of two glutathiones. Mutagenesis data on a variety of poplar glutaredoxins suggest that the incorporation of an iron–sulfur cluster could be a general feature of plant glutaredoxins possessing a glycine adjacent to the catalytic cysteine. In light of these results, the possible involvement of plant glutaredoxins in oxidative stress sensing or iron–sulfur biosynthesis is discussed with respect to their intracellular localization.

scholarly journals Cu+-specific CopB transporter: Revising P1B-type ATPase classification

2018 ◽  
Vol 115 (9) ◽  
pp. 2108-2113 ◽  
Author(s):  
Rahul Purohit ◽  
Matthew O. Ross ◽  
Sharon Batelu ◽  
April Kusowski ◽  
Timothy L. Stemmler ◽  
...  
Keyword(s):  
Maximal Activity ◽  
Spectroscopic Characterization ◽  
Spectroscopic Studies ◽  
Divalent Metal Ions ◽  
X Ray ◽  
Reducing Environment ◽  
Methionine Residues ◽  
Cellular Copper ◽  
X Ray Absorption

The copper-transporting P1B-ATPases, which play a key role in cellular copper homeostasis, have been divided traditionally into two subfamilies, the P1B-1-ATPases or CopAs and the P1B-3-ATPases or CopBs. CopAs selectively export Cu+ whereas previous studies and bioinformatic analyses have suggested that CopBs are specific for Cu2+ export. Biochemical and spectroscopic characterization of Sphaerobacter thermophilus CopB (StCopB) show that, while it does bind Cu2+, the binding site is not the prototypical P1B-ATPase transmembrane site and does not involve sulfur coordination as proposed previously. Most important, StCopB exhibits metal-stimulated ATPase activity in response to Cu+, but not Cu2+, indicating that it is actually a Cu+ transporter. X-ray absorption spectroscopic studies indicate that Cu+ is coordinated by four sulfur ligands, likely derived from conserved cysteine and methionine residues. The histidine-rich N-terminal region of StCopB is required for maximal activity, but is inhibitory in the presence of divalent metal ions. Finally, reconsideration of the P1B-ATPase classification scheme suggests that the P1B-1- and P1B-3-ATPase subfamilies both comprise Cu+ transporters. These results are completely consistent with the known presence of only Cu+ within the reducing environment of the cytoplasm, which should eliminate the need for a Cu2+ P1B-ATPase.

Electrochemical, spectroelectrochemical and ESR spectroscopic characterization of 2,3- and 3,4-cobalt tetrapyridoporphyrazine isomers in non-aqueous media

2009 ◽  
Vol 13 (08n09) ◽  
pp. 876-887 ◽  
Author(s):  
Jianguo Shao ◽  
Juliette Commodore ◽  
Baocheng Han ◽  
Cynthia Pruente ◽  
Christopher A. Hansen
Keyword(s):  
Dimethyl Sulfoxide ◽  
Aqueous Media ◽  
Spectroscopic Characterization ◽  
Spectroscopic Properties ◽  
Axial Ligand ◽  
Electron Transfer Mechanism ◽  
Axial Ligands ◽  
Uv Visible ◽  
High Concentrations

Two cobalt porphyrazines, 2,3-tetrapyridoporphyrazine and 3,4-tetrapyridoporphyrazine, were examined in N,N-dimethylformamide, dimethyl sulfoxide and pyridine solutions as to their electrochemical, spectroelectrochemical and ESR spectroscopic properties. These results were compared with those of the unsubstituted cobalt phthalocyanine. At high concentrations, aggregation was observed for each investigated compound in the three solvents. The intensity of ESR signals of each derivative depends upon the extent of aggregation in its solution. The g values shift towards high field with an increase in the strength of the axial ligand and the number of axial ligands on the cobalt center. Both tetrapyridoporphyrazine complexes undergo one oxidation and three reductions in N,N-dimethylformamide, dimethyl sulfoxide or pyridine solution. Thin-layer UV-visible spectroelectrochemical results confirmed that the first oxidation and first reduction of both compounds are metal-centered while the second and third reductions are ring-centered. An overall electron transfer mechanism for both porphyrazine derivatives is proposed.

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