Kinetics of protein synthesis by polyribosomes

1965 ◽  
Vol 9 (1) ◽  
pp. 16-36 ◽  
Author(s):  
I. Gerst ◽  
S.N. Levine
Keyword(s):  
Protein Synthesis ◽  
Kinetics Of ◽  
Kinetics Of Protein Synthesis

Kinetics of Protein Synthesis in Enucleate Frog Oocytes

Science ◽  
1968 ◽  
Vol 160 (3832) ◽  
pp. 1115-1117 ◽  
Author(s):  
R. E. Ecker ◽  
L. D. Smith ◽  
S. Subtelny
Keyword(s):  
Protein Synthesis ◽  
Kinetics Of ◽  
Kinetics Of Protein Synthesis

scholarly journals Decomposition of time-dependent fluorescence signals reveals codon-specific kinetics of protein synthesis

2018 ◽  
Vol 46 (22) ◽  
pp. e130-e130 ◽  
Author(s):  
Nadin Haase ◽  
Wolf Holtkamp ◽  
Reinhard Lipowsky ◽  
Marina Rodnina ◽  
Sophia Rudorf
Keyword(s):  
Protein Synthesis ◽  
Time Dependent ◽  
Kinetics Of ◽  
Kinetics Of Protein Synthesis

scholarly journals STUDIES ON THE KINETICS OF PROTEIN SYNTHESIS IN YEAST

1961 ◽  
Vol 47 (9) ◽  
pp. 1415-1423 ◽  
Author(s):  
R. J. Young ◽  
H. K. Kihara ◽  
H. O. Halvorson
Keyword(s):  
Protein Synthesis ◽  
Kinetics Of ◽  
Kinetics Of Protein Synthesis

scholarly journals Decomposition of time-dependent fluorescence signals reveals codon-specific kinetics of protein synthesis

2018 ◽  
Vol 46 (22) ◽  
pp. 12186-12187 ◽  
Author(s):  
Nadin Haase ◽  
Wolf Holtkamp ◽  
Reinhard Lipowsky ◽  
Marina Rodnina ◽  
Sophia Rudorf
Keyword(s):  
Protein Synthesis ◽  
Time Dependent ◽  
Kinetics Of ◽  
Kinetics Of Protein Synthesis

scholarly journals Deducing the Kinetics of Protein Synthesis In Vivo from the Transition Rates Measured In Vitro

2014 ◽  
Vol 10 (10) ◽  
pp. e1003909 ◽  
Author(s):  
Sophia Rudorf ◽  
Michael Thommen ◽  
Marina V. Rodnina ◽  
Reinhard Lipowsky
Keyword(s):  
Protein Synthesis ◽  
Transition Rates ◽  
Kinetics Of ◽  
Kinetics Of Protein Synthesis

scholarly journals Preparation and partial characterization of cell-free protein-synthesizing extracts from Tetrahymena pyriformis

1981 ◽  
Vol 194 (3) ◽  
pp. 761-770 ◽  
Author(s):  
E T David ◽  
K E Smith
Keyword(s):  
Protein Synthesis ◽  
Tetrahymena Pyriformis ◽  
Partial Characterization ◽  
Free Protein ◽  
Optimum Synthesis ◽  
Kinetics Of ◽  
Cell Free Protein Synthesis ◽  
Kinetics Of Protein Synthesis

1. We have examined methods necessary for preparing post-mitochondrial supernatants from Tetrahymena pyriformis strain HSM that are capable of efficient cell-free protein synthesis. 2. The requirements for optimum synthesis in these extracts are described. 3. Data relating to the kinetics of protein synthesis and the initiation capacity of these supernatants are presented.

scholarly journals Use of multiple T cell-directed intact ricin immunotoxins for autologous bone marrow transplantation

Blood ◽  
1985 ◽  
Vol 66 (3) ◽  
pp. 627-635 ◽  
Author(s):  
RC Stong ◽  
F Uckun ◽  
RJ Youle ◽  
JH Kersey ◽  
DA Vallera
Keyword(s):  
Protein Synthesis ◽  
T Cell ◽  
Autologous Bone Marrow Transplantation ◽  
Autologous Transplantation ◽  
Leukemic Cells ◽  
Target Antigen ◽  
Target Cells ◽  
Hematopoietic Stem ◽  
Kinetics Of ◽  
Kinetics Of Protein Synthesis

The monoclonal antibodies (MoAb) T101, G3.7, 35.1, and TA-1 were conjugated to intact ricin using a thioether linkage. These MoAb detect, respectively, the CD5[gp67], CD7[p41], CD2[p50], and [gp95, 170] determinants that are found in the vast majority of cases of T cell acute lymphocytic leukemia (T-ALL). The resulting immunotoxins (ITs) and an equimolar mixture of these ITs were evaluated as potential purgative reagents for autologous transplantation in T-ALL. Leukemic cell lines were used to compare the kinetics of protein synthesis inactivation mediated by each IT. The cells were treated with IT in the presence of lactose in order to block the native binding of ricin. The observed rates of protein synthesis inactivation correlated with target antigen expression detected by fluorescence-activated cell sorter analysis. Of the four ITs, T101-ricin (T101-R) exhibited the fastest rate of inactivation, followed in order by G3.7-ricin, TA-1-ricin, and 35.1-ricin. At concentrations greater than 300 ng/mL, a cocktail containing an equimolar amount of all four ITs (referred to as the four- IT cocktail) exhibited kinetics that were as fast or faster than those of T101-R. The long-term cytotoxic effects of individual ITs and the four-IT cocktail were evaluated using a sensitive clonogenic assay. Each IT was specifically cytotoxic and inhibited 1 to 4 logs of clonogenic leukemic cells at doses (300 to 600 ng/mL) that can be used clinically. The four-IT cocktail was highly cytotoxic; a concentration of 300 ng/mL inhibited greater than 4 logs of leukemic cells while sparing the majority of committed (CFU-GM, CFU-E) and pluripotent (CFU- GEMM) hematopoietic stem cells. The determination of both short-term kinetics of protein synthesis inactivation and longer-term inhibition of clonogenic growth allowed new insight into cell killing by IT. Our results suggest that ITs continue to act on clonogenic target cells for a period of three to five days. Interestingly, the four-IT cocktail was not as potent against clonogenic leukemic cells as T101-R alone, although it exhibited kinetics of protein synthesis inhibition that were as fast as those of T101-R alone. This finding suggests that internalized ITs may differ in the length of time they remain active within the cell. Our results also demonstrate the importance of using several different assays to evaluate IT reagents.

Protein synthesis and release by cultured schistosomula ofSchistosoma mansoni

Parasitology ◽  
1993 ◽  
Vol 107 (3) ◽  
pp. 265-274 ◽  
Author(s):  
R. Harrop ◽  
R. A. Wilson
Keyword(s):  
Protein Synthesis ◽  
Protective Immunity ◽  
Soluble Fraction ◽  
Activity Analysis ◽  
Before And After ◽  
Kinetics Of ◽  
Specific Synthesis ◽  
Kinetics Of Protein Synthesis

SummaryThe lung schistosomulum ofSchistosoma mansoniis the target of protective immunity in mice singly vaccinated with irradiated cercariae. Since the effector responses are T cell-mediated, their initiation requires the release of antigens from the intact parasite. We have used the technique of biosynthetic labelling with ‘35S’methionine, before and after transformation of the cercariae, to analyse the kinetics of protein synthesis and release by the schistosomulum. In addition, the proteins present in the soluble fraction of the parasite and those released duringin vitroculture have been characterized. During a 7-day culture period schistosomula derived from labelled cercariae lost proteins most rapidly within the first 3 h after transformation. Two proteins of molecular weight 61 and 20 kDa were dominant and may correspond to areas of proteolytic activity. Analysis of the rate of protein synthesis of schistosomula labelled after transformation revealed four different phases, which may relate to the developmental processes occurringin vivo. During the first 24 h, synthesis was very low, increasing to a plateau and then rising to a peak at day 8; thereafter the rate declined rapidly. Whilst some stage-specific synthesis of proteins was detected in the soluble fractions of the parasite bodies, the pattern of proteins released by cultured larvae was remarkably uniform. At least 15 proteins were detected by autoradiography with bands at 61, 45 and 20 kDa being particularly prominent. These proteins merit further study as potential mediators of the protective immune response.

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