Protein synthesis in resting and stimulated human lymphocytes
The ribosomal profiles in lysates from resting and phytohemagglutinin stimulated human lymphocytes have been analyzed by sucrose gradient centrifugation. The percentage of polyribosomes increased during lymphocyte transformation reaching a maximal value of 60 to 70% of the total ribosomes after 72 h...
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todo:paper_03008177_v16_n2-3_p105_Burrone2023-10-03T15:17:41Z Protein synthesis in resting and stimulated human lymphocytes Burrone, O. Algranati, I.D. phytohemagglutinin in vitro study lymphocyte activation normal human polysome protein synthesis theoretical study Antibiotics Cells, Cultured Chloramphenicol Cycloheximide DNA Human Kinetics Lectins Lymphocyte Activation Lymphocytes Magnesium Poly U Proteins Puromycin Ribosomes RNA, Messenger Translation, Genetic The ribosomal profiles in lysates from resting and phytohemagglutinin stimulated human lymphocytes have been analyzed by sucrose gradient centrifugation. The percentage of polyribosomes increased during lymphocyte transformation reaching a maximal value of 60 to 70% of the total ribosomes after 72 hours of mitogen addition. This time period coincides with maximal in vivo protein synthesis. On the other hand, in nonstimulated lymphocytes, about 25% of the ribosomal particles appeared as aggregates, independently of the incubation period. Experiments performed with homologous cell free systems containing ribosomes and supernatant fluids prepared from unstimulated or activated lymphocytes demonstrate that the mixtures containing both components from stimulated lymphocytes are several fold more active in polypeptide synthesis than the systems which contain ribosomal particles and cell sap from resting cells. Assays carried out with mixtures combining the components from both sources indicate that the increased activity depends on ribosomes as well as on the supernatant fractions. © 1977 Dr. W. Junk b.v. Publishers. Fil:Burrone, O. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Algranati, I.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_03008177_v16_n2-3_p105_Burrone |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
phytohemagglutinin in vitro study lymphocyte activation normal human polysome protein synthesis theoretical study Antibiotics Cells, Cultured Chloramphenicol Cycloheximide DNA Human Kinetics Lectins Lymphocyte Activation Lymphocytes Magnesium Poly U Proteins Puromycin Ribosomes RNA, Messenger Translation, Genetic |
| spellingShingle |
phytohemagglutinin in vitro study lymphocyte activation normal human polysome protein synthesis theoretical study Antibiotics Cells, Cultured Chloramphenicol Cycloheximide DNA Human Kinetics Lectins Lymphocyte Activation Lymphocytes Magnesium Poly U Proteins Puromycin Ribosomes RNA, Messenger Translation, Genetic Burrone, O. Algranati, I.D. Protein synthesis in resting and stimulated human lymphocytes |
| topic_facet |
phytohemagglutinin in vitro study lymphocyte activation normal human polysome protein synthesis theoretical study Antibiotics Cells, Cultured Chloramphenicol Cycloheximide DNA Human Kinetics Lectins Lymphocyte Activation Lymphocytes Magnesium Poly U Proteins Puromycin Ribosomes RNA, Messenger Translation, Genetic |
| description |
The ribosomal profiles in lysates from resting and phytohemagglutinin stimulated human lymphocytes have been analyzed by sucrose gradient centrifugation. The percentage of polyribosomes increased during lymphocyte transformation reaching a maximal value of 60 to 70% of the total ribosomes after 72 hours of mitogen addition. This time period coincides with maximal in vivo protein synthesis. On the other hand, in nonstimulated lymphocytes, about 25% of the ribosomal particles appeared as aggregates, independently of the incubation period. Experiments performed with homologous cell free systems containing ribosomes and supernatant fluids prepared from unstimulated or activated lymphocytes demonstrate that the mixtures containing both components from stimulated lymphocytes are several fold more active in polypeptide synthesis than the systems which contain ribosomal particles and cell sap from resting cells. Assays carried out with mixtures combining the components from both sources indicate that the increased activity depends on ribosomes as well as on the supernatant fractions. © 1977 Dr. W. Junk b.v. Publishers. |
| format |
JOUR |
| author |
Burrone, O. Algranati, I.D. |
| author_facet |
Burrone, O. Algranati, I.D. |
| author_sort |
Burrone, O. |
| title |
Protein synthesis in resting and stimulated human lymphocytes |
| title_short |
Protein synthesis in resting and stimulated human lymphocytes |
| title_full |
Protein synthesis in resting and stimulated human lymphocytes |
| title_fullStr |
Protein synthesis in resting and stimulated human lymphocytes |
| title_full_unstemmed |
Protein synthesis in resting and stimulated human lymphocytes |
| title_sort |
protein synthesis in resting and stimulated human lymphocytes |
| url |
http://hdl.handle.net/20.500.12110/paper_03008177_v16_n2-3_p105_Burrone |
| work_keys_str_mv |
AT burroneo proteinsynthesisinrestingandstimulatedhumanlymphocytes AT algranatiid proteinsynthesisinrestingandstimulatedhumanlymphocytes |
| _version_ |
1807321861577506816 |