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1.
Inorg Chem ; 39(24): 5424-5, 2000 Nov 27.
Artículo en Inglés | MEDLINE | ID: mdl-11154554
2.
J Biochem ; 97(6): 1831-3, 1985 Jun.
Artículo en Inglés | MEDLINE | ID: mdl-3897216

RESUMEN

Magnetization and magnetic susceptibility measurements revealed that the hydrogenase [EC 1.12.2.1] from Desulfovibrio vulgaris Miyazaki F has an independent unpaired electron in its iron-sulfur cluster. The paramagnetic center of the Desulfovibrio hydrogenase is, therefore, different from that in the Chromatium hydrogenase which interacts with another paramagnetic center, probably nickel.


Asunto(s)
Desulfovibrio/enzimología , Hidrogenasas/análisis , Proteínas Hierro-Azufre/análisis , Magnetismo , Modelos Químicos , Temperatura
3.
Nucleic Acids Res ; 12(21): 8029-41, 1984 Nov 12.
Artículo en Inglés | MEDLINE | ID: mdl-6095185

RESUMEN

We have isolated a cDNA clone encoding salmon proopiomelanocortin precursor. Polyadenylated RNA was isolated from pituitary neurointermediate lobes and used to construct a cDNA library. The library was screened with 17 mer of oligodeoxyribonucleotides specific for the hexapeptide sequence in salmon beta-endorphin I, Phe-Met-Lys-Pro-Tyr-Thr at positions 4-9 excluding the third nucleotide. One positive clone, pSSM17 containing an insert of 1303 base pairs (bp) was characterized. Sequence determination revealed that it possessed sequences covering the entire regions encoding ACTH and beta-lipotropin and that the mRNA had the same overall organization as those of other mammalian species, i.e., the following peptide hormones were arranged in order from 5' upstream, ACTH including alpha-melanotropin and corticotropin-like intermediate lobe peptide, beta-lipotropin including gamma-lipotropin, beta-melanotropin and beta-endorphin. Amino acid sequences for putative salmon ACTH, beta-, and gamma-lipotropin were predicted. Comparison of the salmon mRNA sequence with those of mammals showed that the regions of alpha- and beta-MSH are relatively homologous, but other regions are much less so, especially in the 3' nontranslated region where it is much longer and completely heterologous.


Asunto(s)
Clonación Molecular , ADN/metabolismo , Proopiomelanocortina/genética , Secuencia de Aminoácidos , Animales , Secuencia de Bases , Bovinos , Enzimas de Restricción del ADN , Humanos , Hibridación de Ácido Nucleico , Plásmidos , Salmón , Especificidad de la Especie , Porcinos
4.
Biochem Biophys Res Commun ; 122(2): 556-62, 1984 Jul 31.
Artículo en Inglés | MEDLINE | ID: mdl-6087806

RESUMEN

Heterogeneity of salmon pituitary proopiomelanocortin (POMC) mRNA was shown by comparison of the nucleotide sequence of independently isolated cDNA clones encoding POMC, pSSM90, pSSM53 and pSSM17, the last of which was previously characterized. Newly isolated clones pSSM90 and pSSM53 contained inserts of 1228 and 666 base pairs, respectively (excluding poly(A)). Sequence analysis revealed that the former contained sequences coding for the carboxy half of putative corticotropin (ACTH), the whole region of beta-lipotropin (beta-LPH), and the entire 3' nontranslated region, while the latter contained only the 3' nontranslated region. Sequence comparison of the three clones revealed that there are some definite nucleotide changes in the 3' nontranslated regions, i.e., base replacements and base additions at multiple sites, whereas no single change was observed in the coding regions, thus demonstrating heterogeneity and hence polymorphism of the gene in the salmon genome.


Asunto(s)
Hormona Adrenocorticotrópica/genética , Genes , Hormonas Adenohipofisarias/genética , Polimorfismo Genético , Precursores de Proteínas/genética , ARN Mensajero/genética , beta-Lipotropina/genética , Secuencia de Aminoácidos , Animales , Secuencia de Bases , Clonación Molecular , ADN/metabolismo , Enzimas de Restricción del ADN , Proopiomelanocortina , Biosíntesis de Proteínas , Salmón
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