3 results
Search Results
2. Incorporation of N-formylmethionine into peptides by Pseudomonas aeruginosa extracts
- Author
-
Lloyd K. Migita and Roy H. Doi
- Subjects
Electrophoresis ,Paper ,Peptide Biosynthesis ,Reticulocytes ,Formates ,Biology ,Tritium ,medicine.disease_cause ,Biochemistry, Genetics and Molecular Biology (miscellaneous) ,Cell-free system ,chemistry.chemical_compound ,Adenosine Triphosphate ,Folic Acid ,Methionine ,Ribonucleases ,RNA, Transfer ,Transferases ,medicine ,Protein biosynthesis ,Magnesium ,Amino Acids ,Tetrahydrofolic acid ,chemistry.chemical_classification ,Carbon Isotopes ,Chromatography ,Cell-Free System ,Pseudomonas aeruginosa ,N-Formylmethionine ,Amino acid ,Quaternary Ammonium Compounds ,Chloramphenicol ,chemistry ,Biochemistry ,Puromycin - Abstract
A cell-free system capable of carrying out amino acid incorporation into peptides was developed from exponentially growing cultures of Pseudomonas aeruginosa . The amino acid incorporation activity required an ATP energy generating system, Mg 2+ , NH 4 + , tRNA and an amino acid mixture for maximum activity. Ribonuclease, puromycin and chloramphenicol inhibited protein synthesis. N -Formylmethionyl-tRNA was synthesized with a P. aeruginosa enzyme system, methionine, P. aeruginosa tRNA, formate and tetrahydrofolic acid. N -formylmethionine was incorporated into peptides by the P. aeruginosa cell-free system. These results indicate that P. aeruginosa extracts contain methionyl-tRNA transformylase and the complete system for the incorporation of N -formylmethionine into peptides.
- Published
- 1970
3. Changes in haem synthesis associated with occupational exposure to organic and inorganic sulphides
- Author
-
Heikki Savolainen, R. Tenhunen, and P. Jäppinen
- Subjects
Paper ,Occupational Medicine ,Erythrocytes ,Reticulocytes ,Erythrocyte protoporphyrin ,chemistry.chemical_element ,Air Pollutants, Occupational ,Heme ,Hydrogen sulphide ,030226 pharmacology & pharmacy ,01 natural sciences ,03 medical and health sciences ,0302 clinical medicine ,Mole ,Humans ,Hydrogen Sulfide ,Sulfhydryl Compounds ,Air Pollutants ,ATP synthase ,biology ,010401 analytical chemistry ,General Medicine ,Middle Aged ,In vitro ,0104 chemical sciences ,Biochemistry ,chemistry ,biology.protein ,Occupational exposure ,Selenium ,Ferrochelatase ,5-Aminolevulinate Synthetase - Abstract
1. Analysis of reticulocytes for δ-aminolaevulinic acid synthase (AmLev synthase, EC 2.3.1.37) and haem synthase (EC 4.99.1.1) activity in 17 workers in pulp production with low-level hydrogen sulphide and methylmercaptan exposure showed decreased activities in eight and six cases respectively. 2. Erythrocyte protoporphyrin concentration was below the control range in seven cases. 3. Low AmLev synthase and haem synthase activities were found in one patient with hydrogen sulphide intoxication 1 week after the event. The activities had returned to the control levels 2 months later, though erythrocyte protoporphyrin remained abnormally low. 4. In vitro, hydrogen sulphide inhibited haem synthase with an apparent Kl of 3.4 mmol/l. Sulphide anion, on the other hand, inhibited AmLev synthase activity 85% at 10 mmol/l concentration. Thiosulphate anion inhibited AmLev synthase activity 18% (Kl 27 mmol/l) and haem synthase activity 43% at 10 mmol/l concentration. Selenite inhibited AmLev synthase (Kl 5.1 mmol/l) and haem synthase (Kl 9.0 mmol/l). 5. The assay of AmLev synthase and haem synthase could be a valuable addition to the assessment of workers' health in industries generating hydrogen sulphide or/and methylmercaptan, although the mechanism of the toxic effect remains speculative.
- Published
- 1983
Discovery Service for Jio Institute Digital Library
For full access to our library's resources, please sign in.