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Strana 1 od 217 výsledky
Tyrosine-phosphorylated bacterial proteins: Trojan horses for the host cell.
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Acetylation of the tyrosine residues of horse heart cytochrome C.
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Amino acid sequence of horse colipase B.
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The complete sequence of the 96 residues composing horse colipase B has been determined by automated analysis of the intact protein, of two CNBr peptides and two tryptic peptides arising, respectively, from the citraconylated chain and from the unreduced protein. The single histidine of the protein
Specific electrochemical nitration of horse heart myoglobin.
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Earlier findings on electronitration of hen egg-white lysozyme demonstrated a product which was mononitrated at Tyr23, by ion-exchange chromatography, absorbance at 430 nm, dithionite reduction, and Edman sequencing of a nitrated proteolytic peptide. However, the whole protein was not sequenced;
Neuromelanin in the substantia nigra of adult horses.
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The structure and histochemical properties of neuromelanin in the Substantia nigra of the horse were studied by light and electron microscopy. Morphological, histochemical and cytochemical evidences showed the presence of a melanin component in some pigment granules, even if a large quantity of
Structural heterogeneity and subunit composition of horse ferritins.
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Structural, spectroscopic, and immunological properties of horse ferritins extracted from spleen, liver, and heart were studied to test the hypothesis that the different tissue ferritins are hybrids composed of variable proportions of two subunit types. The weight-average molecular weights
Intrinsic fluorescence of a protein devoid of tyrosine and tryptophan: horse hepatocuprein.
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Spectral studies of horse heart porphyrin cytochrome c.
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Removal of the heme iron from cytochrome c to generate porphyrin cytochrome c relieves the quenching of porphyrin fluorescence and enhances the fluorescence of the single tryptophan residue and the 4 tyrosine residues. The intensity of the porphyrin fluorescence is not perturbed by denaturation of
Sympathetic innervation of the ileocecal junction in horses.
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The distribution and chemical phenotypes of sympathetic and dorsal root ganglion (DRG) neurons innervating the equine ileocecal junction (ICJ) were studied by combining retrograde tracing and immunohistochemistry. Immunoreactivity (IR) for tyrosine hydroxylase (TH), dopamine beta-hydroxylase (DBH),
Ionization of tyrosine and lysine residues in native and modified horse cytochrome c.
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1H-n.m.r. and 13C-n.m.r. spectroscopy of horse cytochrome c and 1H-n.m.r. spectroscopy of the lysine-modified proteins N epsilon-acetimidyl-, N epsilon-amidino-, N epsilon-trifluoroacetyl- and N epsilon-maleyl-cytochrome c have shown that, although the lysine modifications do not greatly perturb the
The complete amino acid sequence of horse muscle acylphosphatase.
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The amino acid sequence of horse muscle acylphosphatase is given in the present paper. The carboxymethylated enzyme consists of a single polypeptide chain of 98 amino acid residues with an acetyl group blocking the NH2 terminus and a tyrosine at the COOH terminus. The calculated molecular weight of
Hydrogen ion interactions of horse spleen ferritin and apoferritin.
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The interactions of horse spleen ferritin and its derivative apoferritin with H+ ions were studied by potentiometric and spectrophotometric titration; to aid in data analysis, heats of ionization over a limited pH range and amide content were also determined. Per apoferritin subunit, all tyrosine
Regulatory pathway analysis of coat color genes in Mongolian horses.
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BACKGROUND
Studies on the molecular genetics of horse skin pigmentation have typically focused on very few genes and proteins. In this study, we used Illumina sequencing to determine the global gene expression profiles in horses with white-colored coats and those with black-colored coats, with the
Titration behavior of individual tyrosine residues of myoglobins from sperm whale, horse, and red kangaroo.
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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
Lactoperoxidase-catalyzed iodination of horse cytochrome c:monoiodotyrosyl 74 cytochrome c.
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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
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