The Journal of biological chemistry.
Publisher:
American Society for Biochemistry and Molecular Biology. [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology (2021)
Frequency: Weekly, 1994-
Country: United States
Language: English
Author(s):
American Society of Biological Chemists., American Society of Biological Chemists., Rockefeller Institute for Medical Research.
Start Year:1905 -
ISSN:
0021-9258 (Print)
1083-351X (Electronic)
1067-8816 (Undetermined)
0021-9258 (Linking)
1083-351X (Electronic)
1067-8816 (Undetermined)
0021-9258 (Linking)
Impact Factor
5.5
2022
| NLM ID: | 341041 |
| (DNLM): | J14380000(s) |
| (OCoLC): | 01782222 |
| Coden: | JBCHA3 |
| LCCN: | 06046735 |
| Classification: | W1 JO564C |
Lactoperoxidase-catalyzed iodination of horse cytochrome c:monoiodotyrosyl 74 cytochrome c. Iodination of horse cytochrome c with the lactoperoxidase-hydrogen peroxide-iodide system results initially in the formation of the monoiodotyrosyl 74 derivative. This singly modified protein was obtained in pure form by ion exchange chromatography and preparative column electrophoresis. It shows an intact 695 nm absorption band, the midpoint potential of the native protein, a nuclear magnetic resonance spectrum which indicates an undisturbed heme crevice structure, a normal reaction with antibodies directed against native horse cytochrome c, and circular dichroic spectra in which the only cha...
Electronic and steric factors affecting ligand binding: horse hemoglobins containing 2,4-dimethyldeuteroheme and 2,4-dibromodeuteroheme. Horse globin has been recombined with 2,4-dimethyldeuteroheme and 2,4-dibromodeuteroheme to yield the corresponding reconstituted hemoglobins, and the ligand binding reactions of these reconstituted hemoglobins have been examined in detail. Both hemoglobins exhibit relatively high n values, but 2,4-dimethyldeuterohemoglobin displays a consistently higher oxygen affinity than native hemoglobin, whereas the oxygen affinity of 2,4-dibromodeuterohemoglobin is consistently lower than that of native hemoglobin. The rate constants l’, and 1’4 for the binding of the first and fourth molecules of C...
Amino acid sequence of phospholipase A2 from horse pancreas. The complete amino acid sequence of phosphlipase A2 (EC 3.1.1.4) from horse pancreas was determined. The protein controls of a single polypeptide chain of 125 amino acids and has a molecular weight of 13,927. The chain is crosslinked by seven disulfide bridges. The sequence was determined by automated Edman degradation of the intact protein and several of the large peptide fragments. Smaller peptides were analyzed by manual Edman degradation. Fragmentation of the peptide chain was accomplished by enzymatic digestion with trypsin, chymotrypsin, and thermolysin. The final overlap was found by di...
Steady state kinetics and binding of eukaryotic cytochromes c with yeast cytochrome c peroxidase. 1. The steady state kinetics for the oxidation of ferrocytochrome c by yeast cytochrome c peroxidase are biphasic under most conditions. The same biphasic kinetics were observed for yeast iso-1, yeast iso-2, horse, tuna, and cicada cytochromes c. On changing ionic strength, buffer anions, and pH, the apparent Km values for the initial phase (Km1) varied relatively little while the corresponding apparent maximal velocities varied over a much larger range. 2. The highest apparent Vmax1 for horse cytochrome c is attained at relatively low pH (congruent to 6.0) and low ionic strength (congruent to...
Transmission of the cytochrome c structural gene in horse-donkey crosses. Donkey cytochrome c was shown to differ from horse cytochrome c by having a serine in position 47 rather than a threonine. The rest of the amino acid sequences are identical. Mules and hinnies, both males and females, carry equal amounts of horse and donkey cytochromes c. The same ratio is found in hinnies in preparations from heart tissue and from skeletal muscle. These results demonstrate that cytochrome c is transmitted in horse-donkey crosses as a simple Mendelian character which is neither sex-linked nor shows dominance. The cytochrome c gene is therefore located in the nuclear genome, as...
Titration behavior of individual tyrosine residues of myoglobins from sperm whale, horse, and red kangaroo. The titration behavior of individual tyrosine residues of myoglobins has been studied by observing the pH dependence of the chemical shifts of Czeta and Cgamma of these residues in natural abundance of 13C Fourier transform NMR spectra (at 15.18 MHz, in 20-mm sample tubes, at 37 degrees) of cyanoferrimyoglobins from sperm whale, horse, and red kangaroo. A comparison of the pH dependence of the spectra of the three proteins yielded specific assignments for the resonance of Tyr-151 (sperm whale) and Tyr-103 (sperm whale and horse). Selective proton decoupling yielded specific assignments for Cze...
Ligand binding properties of horse hemoglobins containing deutero- and mesoheme. The reactions of horse globin reconstituted with proto-, deutero-, and mesoheme have been examined by equilibrium and kinetic methods. In virtually all reactions studied, mesohemoglobin displays the more extreme functional behavior, whereas deuterohemoglobin exhibits behavior which is either very similar to native hemoglobin or intermediate between the two. Our kinetic and equilibrium results indicate that the primary effect of heme modification on the functional properties of hemoglobin is to alter the intrinsic reactivities of the deoxy and liganded conformations. Heme modification does not,...
Differences in subunit composition and iron content of isoferritins. Horse spleen ferritin was fractionated into its constituent isoferritins by isoelectric focusing. Separated isoferritins were stable and showed no tendency to redistribute when re-examined by analytical gel focusing. All of the isoferritins were immunologically indistinguishable when tested with antibodies raised against unfractionated horse spleen ferritin. The separated isoferritins also had similar conformations as determined by circular dichroism. Iron distribution studies, however, revealed a wide disparity among the isoferritins. The most acidic components had the lowest iron content but...
Structure of dermatan sulfate. VII. The copolymeric structure of dermatan sulfate from horse aorta. The structure of dermatan sulfate-chondroitin sulfate
copolymers, isolated from horse aorta, has been examined.
It was found that a large proportion of the galactosaminoglycans of this tissue was obtained as a discrete polysaccharide fraction with an L-iduronic acid to D-glucuronic
acid ratio of approximately 1: 2. This finding together with
infrared data indicated that the polymer contained approximately equimolar proportions of the three repeating disaccharide units glucuronosyl-N-acetylgalactosamine 4-sulfate
(A), iduronosyl-N-acetylgalactosamine 4-sulfate (B), and
glucuronosyl-N-acet...
A comparison of the resistance of human and horse ferrihemoglobin to acid denaturation. Many of the stability characteristics of horse ferrihemo-globin (Hb+) in acid solutions, such as pH dependence and susceptibility to stabilization by iron ligands, are shared by human ferrihemoglobin, but striking differences between the two proteins exist. The most noticeable is the much greater rate of denaturation of the human protein at all pH values. Other differences include a shift to higher pH in the equi-librium between native and acid-denatured forms, differ-ences in the temperature at which the temperature effect on the equilibrium-pH curve reverses, a complete absence in human Hb+ ...