Showing results 81 to 85 of 85
 Nucleotide sequence and amplification in bacteria of structural gene for rat growth hormone; ; Martial, Joseph  et alin Nature (1977), 270(5637), 486-94 The primary structure of DNA containing the sequence for rat pituitary growth hormone mRNA has been determined. DNA was obtained by reverse transcription of polyadenylated RNA from cultured pituitary ... [more ▼] The primary structure of DNA containing the sequence for rat pituitary growth hormone mRNA has been determined. DNA was obtained by reverse transcription of polyadenylated RNA from cultured pituitary cells and from recombinant bacterial plasmids. The amino acid sequences for rat growth hormone and its precursor form have been deduced from the determined nucleotide sequences. [less ▲] Detailed reference viewed: 21 (3 ULg)Construction and analysis of recombinant DNA for human chorionic somatomammotropin; ; Martial, Joseph et alin Nature (1977), 270(5637), 494-499 DNA complementary to mRNA coding for the human polypeptide hormone, chorionic somatomammotropin, has been purified by specific restriction endonuclease digestion and religation before cloning into ... [more ▼] DNA complementary to mRNA coding for the human polypeptide hormone, chorionic somatomammotropin, has been purified by specific restriction endonuclease digestion and religation before cloning into bacterial plasmids. The primary structure of a major portion of this mRNA species is deduced from the nucleotide sequence of the recombinant DNA. [less ▲] Detailed reference viewed: 13 (1 ULg) Fate of thiazolidine ring during fragmentation of penicillin by exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61Frère, Jean-Marie ; Ghuysen, Jean-Marie ; et alin Nature (1976), 260(5550), 451-454 LIKE various beta-lactamases, acylases and esterases1, the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61 degrades benzylpenicillin and other beta-lactam antibiotics2-4. The R61 enzyme ... [more ▼] LIKE various beta-lactamases, acylases and esterases1, the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61 degrades benzylpenicillin and other beta-lactam antibiotics2-4. The R61 enzyme, however, markedly differs from the other penicillin-degrading enzymes in causing fragmentation of the penicillin nucleus. By using 8-14C-benzylpenicillin (benzyl labelled) as substrate, one of the fragments produced was shown to be 14C-phenylacetylglycine5. The reaction with the R61 enzyme is also peculiar in that it is a slow process. This is because of the long half life of the stoichiometnc complex transitorily formed between the antibiotic and the enzyme. Thus, for example, the value of the half life for the complex formed with benzylpenicillin is 80 min in 10 mM phosphate buffer (pH 7.0) and at 37 °C. As breakdown of the complex proceeds, however, phenylacetylglycine (when benzylpenicillin is used as substrate) is released and the enzyme concomitantly recovers its ability to bind penicillin. We have now characterised the fragment (hereby designated as the Y product) arising from the thiazolidine ring of penicillin as a result of the fragmentation of the antibiotic molecule by the R61 enzyme. [less ▲] Detailed reference viewed: 11 (1 ULg)Fragmentation of benzylpenicillin after interaction with the exocellular DD-carboxypeptidase-transpeptidases of Streptomyces R61 and R39Frère, Jean-Marie ; Ghuysen, Jean-Marie ; et alin Nature (1975), 258(5531), 168-170 Detailed reference viewed: 6 (0 ULg)Diffusion of copper in the animal kingdomFredericq, Léon in Nature (1880), XXXI Detailed reference viewed: 3 (2 ULg) |
||
