نتایج جستجو برای: tyr

تعداد نتایج: 6296  

Journal: :The Journal of biological chemistry 1993
S Eriksson B Nordén K Morimatsu T Horii M Takahashi

The tyrosine fluorescence of the RecA protein is quenched by about 15% upon binding of the cofactor analog adenosine 5'-O-(3-thiotriphosphate) (ATP gamma S). This quenching is not observed with a modified RecA in which the tyrosine residue at position 264 (Tyr-264) is replaced for alanine by site-directed mutagenesis, a modification which also results in a decrease of binding affinity of cofact...

Journal: :Nucleic acids research 1988
L C James T A Hughes R Curtiss

5' AAGCTTCCAC TACCTTGCCA CCCGCAATAA GAACGATTAC TTCTCCCTCG CCTT 54 Kec Pro tie Thr Asn 141 CTACCA CCTAAAGATC TCCCTCTTAT TTTTAGOTTG AACTCGTATA AACCAAAATT AATTACACCA GATAAA ATG CCA ATT ACA AAT -35 -10 BBS fut Lys ThT Hec Leu Il« Thr Tyr Ala Aap Ser Leu Gly Lye Asa Leu Lys Glu Leu Asn Glu A«n H e Glu Agn Tyr AAA ACA ATG TTC ATT ACT TAC GCA CAC ACT TTC OGT AAA AAT TTG AAA CAA TTG AAT GAA AAT ATT GAG...

Journal: :The Journal of biological chemistry 1990
T Shimokawa R J Kulmacz D L DeWitt W L Smith

There are spectral and biochemical data suggesting that a tyrosine group(s) is involved in the cyclooxygenase reaction catalyzed by prostaglandin endoperoxide (PGH) synthase. Treatment with tetranitromethane, a reagent which nitrates tyrosine residues, abolishes cyclooxygenase activity, but this inactivation can be largely prevented by competitive cyclooxygenase inhibitors such as ibuprofen and...

Journal: :Protein science : a publication of the Protein Society 1996
E S Eberhardt P K Wittmayer B M Templer R T Raines

An intricate architecture of covalent bonds and noncovalent interactions appear to position the side chain of Lys 41 properly within the active site of bovine pancreatic ribonuclease A (RNase A). One of these interactions arises from Tyr 97, which is conserved in all 41 RNase A homologues of known sequence. Tyr 97 has a solvent-inaccessible side chain that donates a hydrogen bond to the main-ch...

Journal: :The Journal of biological chemistry 1993
M C Wells-Knecht T G Huggins D G Dyer S R Thorpe J W Baynes

The concentrations of ortho-tyrosine (o-Tyr) and dityrosine (DT) were measured in noncataractous human lenses in order to assess the role of protein oxidation reactions in the aging of lens proteins. The measurements were conducted by selected ion monitoring-gas chromatography/mass spectrometry using deuterium-labeled internal standards, which provided both high sensitivity and specificity for ...

Journal: :Food & function 2016
Z Zhang Y Zhao X Wang R Lin Y Zhang H Ma Y Guo L Xu B Zhao

Food-derived bioactive peptides may have various physiological modulatory and regulatory functions and are now being studied extensively. Recently, the novel dipeptide Tyr-Ala was isolated from hydrolyzed maize protein. Tyr-Ala significantly prolonged the lifespan of wild-type Caenorhabditis elegans and extended the nematode healthspan and lifespan during heat/oxidative stress. Compared with it...

Journal: :Journal of nuclear medicine : official publication, Society of Nuclear Medicine 2016
Costanza Santini Joeri Kuil Anton Bunschoten Stefan Pool Erik de Blois Yanto Ridwan Jeroen Essers Monique R Bernsen Fijs W B van Leeuwen Marion de Jong

UNLABELLED In the treatment of neuroendocrine tumors (NETs), complete surgical removal of malignancy is generally desirable, because it offers curative results. Preoperative guidance with radiolabeled somatostatin analogs, commonly used for NET diagnosis and preoperative planning, is limited by its low resolution, with the risk that tumor margins and small metastases will be incompletely resect...

1999
Christopher M. Harris Gianluca Molla Mirella S. Pilone Loredano Pollegioni

We have studied D-amino-acid oxidase from Rhodotorula gracilis by site-directed mutagenesis for the purpose of determining the presence or absence of residues having a possible role in acid/base catalysis. Tyr-223, one of the very few conserved residues among D-aminoacid oxidases, has been mutated to phenylalanine and to serine. Both mutants are active catalysts in turnover with D-alanine, and ...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1991
N Chartrel J M Conlon J M Danger A Fournier M C Tonon H Vaudry

A polypeptide was purified from frog brain extracts on the basis of its ability to inhibit alpha-melanotropin release from perifused frog neurointermediate lobes. Based on Edman degradation, amino acid analysis, and peptide mapping, the primary structure of this frog melanotropin-release-inhibiting factor (melanostatin) was determined to be H-Tyr-Pro-Ser-Lys-Pro-Asp-Asn-Pro-Gly-Glu-Asp-Ala-Pro-...

2001
Ted J. Ebersole J. Michael Conlon Frederick W. Goetz Sunny K. Boyd

Neuropeptide Y (NPY) from the brain of an amphibian from the order Gymnophiona (the caecilian, Typhlonectes natans) was characterized. We cloned a 790 base pair cDNA encoding the caecilian NPY precursor. The open reading frame consisted of 291 bases, indicating an NPY precursor of 97 amino acids. Both deduced and isolated NPY primary structures were Tyr-Pro-Ser-Lys-Pro-Asp-AsnPro-Gly-Glu-Asp-Al...

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