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Monoclonal and polyclonal xenoantibodies to the HLA-A, B, C antigenic molecular complex do not affect the functional activity of C3 receptors.
Indiveri F, Pellegrino MA, Quaranta V, Molinaro GA, Ferrone S
(1980) Immunobiology 158: 17-21
MeSH Terms: Animals, Antibodies, Antigen-Antibody Complex, Clone Cells, Complement C3, HLA Antigens, Haplorhini, Horses, Humans, Immune Sera, Receptors, Complement, Rosette Formation, Sheep
Added March 27, 2014
1 Communities
1 Members
0 Resources
13 MeSH Terms
The presteady state reaction of chemically modified cytochromes c with cytochrome oxidase.
Veerman EC, Wilms J, Dekker HL, Muijsers AO, van Buuren KJ, van Gelder BF, Osheroff N, Speck SH, Margoliash E
(1983) J Biol Chem 258: 5739-45
MeSH Terms: Animals, Cattle, Cytochrome c Group, Electron Transport Complex IV, Horses, Kinetics, Mathematics, Osmolar Concentration, Temperature
Added March 5, 2014
0 Communities
1 Members
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9 MeSH Terms
Definition of cytochrome c binding domains by chemical modification. Interaction of horse cytochrome c with beef sulfite oxidase and analysis of steady state kinetics.
Speck SH, Koppenol WH, Dethmers JK, Osheroff N, Margoliash E, Rajagopalan KV
(1981) J Biol Chem 256: 7394-400
MeSH Terms: Affinity Labels, Animals, Binding Sites, Cattle, Cytochrome c Group, Horses, Kinetics, Liver, Models, Molecular, Osmolar Concentration, Oxidoreductases, Oxidoreductases Acting on Sulfur Group Donors, Protein Binding, Protein Conformation
Added March 5, 2014
0 Communities
1 Members
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14 MeSH Terms
Mapping of anion binding sites on cytochrome c by differential chemical modification of lysine residues.
Osheroff N, Brautigan DL, Margoliash E
(1980) Proc Natl Acad Sci U S A 77: 4439-43
MeSH Terms: Animals, Anions, Binding Sites, Carbonates, Cytochrome c Group, Dinitrobenzenes, Horses, Lysine, Phosphates, Structure-Activity Relationship, Trinitrobenzenes
Show Abstract · Added March 5, 2014
The carbonate binding site on horse cytochrome c was mapped by comparing the yields of carboxydinitrophenyl-cytochromes c, each with a single carboxydinitrophenyl-substituted lysine residue per molecule, when the modification reaction was carried out in the presence and absence of carbonate. The site is located on the "left surface" of the protein and consists of lysine residues 72 and/or 73 as well as 86 and/or 87 (Carbonate Site). Although one of the binding sites for phosphate on cytochrome c (Phosphat Site I) is located near the carbonate site, the sites are distinctly different since carbonate does not displace bound phosphate, as monitored by 31P NMR. Furthermore, citrate interacts with Phosphate Site I with high affinity, whereas chloride, acetate, borate, and cacodylate have a much lower affinity for this site, if they bind to it at all. The affinity of phosphate for Phosphate Site I (KD = 2 X 10(-4) M) is at least 1 order of magnitude higher than it is for other sites of interaction.
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11 MeSH Terms
Definition of enzymic interaction domains on cytochrome c. Purification and activity of singly substituted carboxydinitrophenyl-lysine 7, 25, 73, 86, and 99 cytochromes c.
Osheroff N, Brautigan DL, Margoliash E
(1980) J Biol Chem 255: 8245-51
MeSH Terms: Animals, Cattle, Cytochrome c Group, Dinitrophenols, Electron Transport Complex IV, Horses, Kinetics, Lysine, Magnetic Resonance Spectroscopy, Mitochondria, Heart, Models, Molecular, Oxidation-Reduction, Potentiometry, Protein Binding, Protein Conformation, Submitochondrial Particles
Added March 5, 2014
0 Communities
1 Members
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16 MeSH Terms
Electrostatic interactions in cytochrome c. The role of interactions between residues 13 and 90 and residues 79 and 47 in stabilizing the heme crevice structure.
Osheroff N, Borden D, Koppenol WH, Margoliash E
(1980) J Biol Chem 255: 1689-97
MeSH Terms: Animals, Computers, Cytochrome c Group, Dinitrophenols, Drug Stability, Haplorhini, Heme, Horses, Humans, Hydrogen-Ion Concentration, Lysine, Models, Molecular, Myocardium, Protein Binding, Protein Conformation, Species Specificity, Spectrophotometry, Trinitrobenzenes
Added March 5, 2014
0 Communities
1 Members
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18 MeSH Terms
Chemical and physical properties of serum transferrins from several species.
Hudson BG, Ono M, Brockway WJ, Castellino FJ
(1973) Biochemistry 12: 1047-53
MeSH Terms: Amino Acids, Animals, Cattle, Electrophoresis, Polyacrylamide Gel, Fucose, Galactose, Glucosamine, Guanidines, Horses, Iron, Mannose, Mercaptoethanol, Molecular Weight, Monosaccharides, Neuraminic Acids, Peptides, Polysaccharides, Protein Binding, Rabbits, Species Specificity, Swine, Transferrin, Ultracentrifugation
Added December 10, 2013
1 Communities
1 Members
0 Resources
23 MeSH Terms
Changes in LH pulse frequency and amplitude in intact mares during the transition into the breeding season.
Fitzgerald BP, Affleck KJ, Barrows SP, Murdoch WL, Barker KB, Loy RG
(1987) J Reprod Fertil 79: 485-93
MeSH Terms: Animals, Female, Horses, Luteinizing Hormone, Reproduction, Seasons, Secretory Rate
Show Abstract · Added May 12, 2010
Two groups of mares were exposed to an abrupt, artificial increase or a natural increase in daylength. In both groups, mean LH pulse frequency increased with time of year and was accompanied by a reciprocal decrease in LH pulse amplitude. A non-pulsatile pattern of LH secretion was observed in some mares sampled close to the day of ovulation. Maximum mean LH pulse frequency and the onset of the breeding season occurred earlier in those mares exposed to an abrupt artificial increase in daylength. In blood samples collected frequently, mean serum LH concentrations increased in relation to time of year. However, during 60 days before ovulation, when LH pulse frequency increased, mean daily serum LH values only increased on Day -3 before ovulation. The magnitude of the periovulatory LH rise was greater before the second than the first ovulation of the breeding season. These results support the hypothesis that, in the mare, a photoperiod-induced seasonal alteration in LH pulse frequency and/or amplitude may play a role in the onset of the breeding season.
0 Communities
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7 MeSH Terms
The identification and formation of 20-aldehyde leukotriene B4.
Soberman RJ, Sutyak JP, Okita RT, Wendelborn DF, Roberts LJ, Austen KF
(1988) J Biol Chem 263: 7996-8002
MeSH Terms: Alcohol Dehydrogenase, Animals, Chromatography, High Pressure Liquid, Cytochrome P-450 Enzyme System, Horses, Humans, Isoenzymes, Leukocytes, Mononuclear, Leukotriene B4, Mass Spectrometry, Microsomes, NADP
Show Abstract · Added December 10, 2013
Microsomes of human polymorphonuclear leukocytes (PMN) in the presence of 100 microM NADPH converted 0.6 microM leukotriene B4 (LTB4) to 20-OH-LTB4 (retention time = 18.0 min) and to two additional compounds designated I (retention time = 16.8 min) and II (retention time = 9.6 min) as analyzed by reverse-phase high performance liquid chromatography (HPLC). Compounds I and II were also formed from the reaction of 1.0 microM 20-OH-LTB4, PMN microsomes, and 100 microM NADPH; the identity of compound II was confirmed as 20-COOH-LTB4 by gas chromatography-mass spectrometry. Equine alcohol dehydrogenase in the presence of 100 microM NAD+ in 0.2 M glycine buffer (pH 10.0) converted 20-OH-LTB4 to 20-aldehyde (CHO) LTB4, which coeluted with compound I on reverse-phase HPLC. In the presence of 100 microM NADH in 50 mM potassium phosphate buffer (pH 6.5), equine alcohol dehydrogenase reduced both 20-CHO-LTB4 and compound I to 20-OH-LTB4, indicating the identity of compound I as 20-CHO-LTB4. Gas chromatography-mass spectrometry of trideuterated O-methyl-oxime trimethylsilyl ether methyl ester derivative of 3H-labeled compound I definitively established compound I as 20-CHO-LTB4. Addition of immune IgG to cytochrome P-450 reductase or 1.0 mM SKF-525A completely inhibited the formation of 20-CHO-LTB4 from 20-OH-LTB4, indicating that the reaction was catalyzed by a cytochrome P-450. LTB5 (3.0 microM), a known substrate for cytochrome P-450LTB and a competitive inhibitor of LTB4 omega-oxidation, completely inhibited the omega-oxidation of 1.5 microM 20-OH-LTB4 to 20-CHO-LTB4, indicating that the cytochrome P-450 was P-450LTB. Conversion of 1.0 microM 20-CHO-LTB4 to 20-COOH-LTB4 by PMN microsomes was also dependent on NADPH and inhibited by antibody to cytochrome P-450 reductase, 1.0 mM SKF-525A, or 5.0 microM LTB5, indicating that this reaction was also catalyzed by cytochrome P-450LTB. These results identify the novel metabolite 20-CHO-LTB4 and indicate that cytochrome P-450LTB catalyzes three sequential omega-oxidations of LTB4 leading to the formation of 20-COOH-LTB4 via 20-OH-LTB4 and 20-CHO-LTB4 intermediates.
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12 MeSH Terms
Follicle-stimulating hormone pulse amplitude decreases with the onset of the breeding season in the mare.
Hines KK, Affleck KJ, Barrows SP, Murdoch WL, Fitzgerald BP, Loy RG
(1991) Biol Reprod 44: 516-21
MeSH Terms: Activity Cycles, Animals, Female, Follicle Stimulating Hormone, Horses, Ovulation, Periodicity, Reproduction, Seasons
Show Abstract · Added May 12, 2010
The relationship between daily mean FSH concentrations in serum and the pattern of FSH detected by frequent sampling for 12-h periods (samples every 15 min) was examined in five mares during the transition into the breeding season. The five mature anestrous mares were exposed to a natural increase in daylength. Blood samples were collected daily from February 1 until the first ovulation of the breeding season (April 14 +/- 3.7 days, Mean +/- SEM). Periods of frequent blood collection were performed every two weeks. Blood samples were obtained daily by jugular venipuncture or jugular cannula (frequent samples). Mean daily concentrations of FSH in serum determined by RIA decreased during seasonal transition. Patterns of FSH in serum detected by frequent sampling were pulsatile. FSH pulse amplitude decreased during seasonal transition, and the decrease in amplitude was associated with the decrease in mean serum FSH concentrations. This decrease in FSH pulse amplitude may reflect an involvement of a follicular product from developing follicles or a change in hypothalamic stimulation of pituitary FSH release.
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9 MeSH Terms