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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Autores principales: Burrone, Oscar R., Algranati, Israel David
Publicado: 1977
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DNA
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03008177_v16_n2-3_p105_Burrone
http://hdl.handle.net/20.500.12110/paper_03008177_v16_n2-3_p105_Burrone
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spelling paper:paper_03008177_v16_n2-3_p105_Burrone2023-06-08T15:27:21Z Protein synthesis in resting and stimulated human lymphocytes Burrone, Oscar R. Algranati, Israel David 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. 1977 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03008177_v16_n2-3_p105_Burrone 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
collection 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, Oscar R.
Algranati, Israel David
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.
author Burrone, Oscar R.
Algranati, Israel David
author_facet Burrone, Oscar R.
Algranati, Israel David
author_sort Burrone, Oscar R.
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
publishDate 1977
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03008177_v16_n2-3_p105_Burrone
http://hdl.handle.net/20.500.12110/paper_03008177_v16_n2-3_p105_Burrone
work_keys_str_mv AT burroneoscarr proteinsynthesisinrestingandstimulatedhumanlymphocytes
AT algranatiisraeldavid proteinsynthesisinrestingandstimulatedhumanlymphocytes
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