scholarly journals In vitro Protein Synthesis by Plastids of Phaseolus vulgaris. II. The Probable Relation Between Ribonuclease Insensitive Amino Acid Incorporation and the Presence of Intact Chloroplasts

1968 ◽  
Vol 43 (4) ◽  
pp. 495-503 ◽  
Author(s):  
Maurice M. Margulies ◽  
Elisabeth Gantt ◽  
Francesco Parenti
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Phaseolus Vulgaris ◽  
Amino Acid Incorporation ◽  
In Vitro Protein Synthesis ◽  
Acid Incorporation ◽  
Intact Chloroplasts ◽  
Probable Relation ◽  
Vitro Protein

Effect of Cycloheximide on In Vitro and In Vivo Protein Synthesis by Certain Tissues of Rats and Pigeons with Special Reference to Muscle

1973 ◽  
Vol 51 (12) ◽  
pp. 933-941 ◽  
Author(s):  
Njanoor Narayanan ◽  
Jacob Eapen
Keyword(s):  
Amino Acids ◽  
Body Weight ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Amino Acid Incorporation ◽  
Contrast Administration ◽  
Acid Incorporation ◽  
Tissue Homogenates

The effect of cycloheximide in vitro and in vivo on the incorporation of labelled amino acids into protein by muscles, liver, kidneys, and brain of rats and pigeons was studied. In vitro incorporation of amino acids into protein by muscle microsomes, myofibrils, and myofibrillar ribosomes was not affected by cycloheximide. In contrast, administration of the antibiotic into intact animals at a concentration of 1 mg/kg body weight resulted in considerable inhibition of amino acid incorporation into protein by muscles, liver, kidneys, and brain. This inhibition was observed in all the subcellular fractions of these tissues during a period of 10–40 min after the administration of the precursor. Tissue homogenates derived from in vivo cycloheximide-treated animals did not show significant alteration in in vitro amino acid incorporation with the exception of brain, which showed a small but significant enhancement.

scholarly journals Action of growth hormone in vitro on the net uptake and incorporation into protein of amino acids in muscle from intact rabbits given protein-deficient diets

1976 ◽  
Vol 35 (1) ◽  
pp. 1-10 ◽  
Author(s):  
M. R. Turner ◽  
P. J. Reeds ◽  
K. A. Munday
Keyword(s):  
Amino Acids ◽  
Growth Hormone ◽  
Protein Synthesis ◽  
Amino Acid ◽  
De Novo ◽  
Amino Acid Uptake ◽  
Acid Uptake ◽  
Amino Acid Incorporation ◽  
Acid Incorporation

1. Net amino acid uptake, and incorporation into protein have been measured in vitro in the presence and absence of porcine growth hormone (GH) in muscle from intact rabbits fed for 5 d on low-protein (LP), protein-free (PF) or control diets.2. In muscle from control and LP animals GH had no effect on the net amino acid uptake but stimulated amino acid incorporation into protein, although this response was less in LP animals than in control animals.3. In muscle from PF animals, GH stimulated both amino acid incorporation into protein and the net amino acid uptake, a type of response which also occurs in hypophysectomized animals. The magnitude of the effect of GH on the incorporation of amino acids into protein was reduced in muscle from PF animals.4. The effect of GH on the net amino acid uptake in PF animals was completely blocked by cycloheximide; the uptake effect of GH in these animals was dependent therefore on de novo protein synthesis.5. It is proposed that in the adult the role of growth hormone in protein metabolism is to sustain cellular protein synthesis when there is a decrease in the level of substrate amino acids, similar to that which occurs during a short-term fast or when the dietary protein intake is inadequate.

scholarly journals Biotin-mediated protein biosynthesis

1974 ◽  
Vol 140 (3) ◽  
pp. 549-556 ◽  
Author(s):  
R. L. Boeckx ◽  
K. Dakshinamurti
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Rat Liver ◽  
Intestinal Mucosa ◽  
Protein Biosynthesis ◽  
Amino Acid Incorporation ◽  
Acid Incorporation ◽  
Stimulation Of

The effect of administration of biotin to biotin-deficient rats on protein biosynthesis was studied. Biotin treatment resulted in stimulation by more than twofold of amino acid incorporation into protein, both in vivo and in vitro in rat liver, pancreas, intestinal mucosa and skin. Analysis of the products of amino acid incorporation into liver proteins in vivo and in vitro indicated that the synthesis of some proteins was stimulated more than twofold, but others were not stimulated at all. This indicates a specificity in the stimulation of protein synthesis mediated by biotin.

In vitro protein synthesis directed by R17 viral ribonucleic acid. II. On the fate of mRNA in the cell-free system

1969 ◽  
Vol 47 (12) ◽  
pp. 1179-1186 ◽  
Author(s):  
Satomi J. Igarashi
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid Incorporation ◽  
Free System ◽  
Cell Free System ◽  
E Coli ◽  
Acid Incorporation ◽  
Binding Factor ◽  
Vitro Protein

In the crude E. coli B cell-free system, mRNA was hydrolyzed by contaminating nuclease activities before significant polymerization of amino acids took place. Ribosomes appeared to be one of the sources of nuclease. A modified high-salt washing procedure was developed to remove nuclease from ribosomes. RNase-free ribosomes thus obtained appeared to be inactive in poly-U-directed phenylalanine incorporation, unless poly-U binding factor was added to the system. R17 RNA could not direct amino acid incorporation in the presence of RNase-free ribosomes because binding of intact R17 RNA to ribosomes did not take place even in the presence of poly-U binding factor.

THYROXINE STIMULATION OF AMINO ACID INCORPORATION INTO MITOCHONDRIAL PROTEIN: DIFFERENCES BETWEEN IN VIVO AND IN VITRO EFFECTS

1973 ◽  
Vol 72 (4) ◽  
pp. 684-696 ◽  
Author(s):  
Amirav Gordon ◽  
Martin I. Surks ◽  
Jack H. Oppenheimer
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Mitochondrial Protein ◽  
Leucine Incorporation ◽  
Mitochondrial Protein Synthesis ◽  
Amino Acid Incorporation ◽  
Acid Incorporation ◽  
Stimulation Of

ABSTRACT The in vivo and in vitro stimulation of rat hepatic mitochondrial protein synthesis by thyroxine (T4) was compared. In confirmation of Buchanan & Tapley (1966). T4 added to isolated mitochondria rapidly stimulated [14C] leucine incorporation into mitochondrial protein. The in vitro stimulation was reversed after T4 was removed by incubating the mitochondria with bovine serum albumin (BSA). The decrease in T4 stimulation of protein synthesis appeared proportional to the T4 removed by BSA. Thus, it appears probable that exchangeable T4 controls the in vitro system. In contrast, the increase in mitochondrial protein synthesis which was observed 3 to 4 days after pretreatment of hypothyroid rats with labelled and non-radioactive T4 was not reversed by BSA treatment. Moreover, mitochondrial radioactivity could not be extracted with albumin. The in vivo phenomenon does not, therefore, appear to be related to exchangeable hormone in the mitochondria. Furthermore, the estimated quantity of T4 associated with mitochondria after in vivo stimulation was at least two orders of magnitude less than that required to produce comparable stimulation of mitochondrial protein synthesis in vitro. These findings strongly suggest that in vitro and in vivo stimulation of amino acid incorporation by T4 may be mediated by different biochemical mechanisms.

Suppressors suaC 109 and suaA 101 of Aspergillus nidulans alter the ribosomal phenotype in vitro

1987 ◽  
Vol 7 (12) ◽  
pp. 941-948 ◽  
Author(s):  
A. Zamir ◽  
S. S. Martinelli
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Aspergillus Nidulans ◽  
Ribosomal Proteins ◽  
Amino Acid Incorporation ◽  
Free System ◽  
Cell Free System ◽  
Translation Factors ◽  
Acid Incorporation

A new homologous, cell-free system for protein synthesis has been devised for use with ribosomes and elongation factors from Aspergillus nidulans. Ribosome preparations from strains with either the suaAlO1 or suaCl09 mutations have a higher misreading ratio (non-cognate:cognate amino acid incorporation) in the presence of hygromycin than controls. They can be classed as fidelity mutants. These results also prove that the mutations must be in genes coding for ribosomal proteins or enzymes which modify ribosomal proteins post-translationally. Alternatively, the genes could code for translation factors.

EFFECT OF IODIDE AND THYROTROPHIN ON IN VITRO 14C-AMINO ACID INCORPORATION INTO RAT THYROID PROTEINS

1974 ◽  
Vol 76 (2) ◽  
pp. 273-285 ◽  
Author(s):  
Lubomir J. Valenta
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Relative Concentration ◽  
Total Radioactivity ◽  
Amino Acid Incorporation ◽  
Control Value ◽  
Acid Incorporation ◽  
Rat Thyroid

ABSTRACT Thyroid lobes from rats on normal (NID) or low iodine (LID) intake were incubated for 4 hours in vitro in the presence of 14C-amino acids. The 14C-amino acid incorporation into thyroid protein was significantly higher in thyroids from LID than from NID fed rats, 7.82 ± 1.01 % (mean ± sd) of total radioactivity of the incubation mixture per 100 mg tissue compared to 3.74 ± 0.60 % respectively. Thyrotrophin (TSH) in vitro did not influence the 14C-amino acid incorporation. Iodide in concentration 10−7 m and higher decreased 14C-radioactivity incorporation into protein by 19.40 ± 3.06 and 26.59 ± 4.06 % of the control value for NID and LID rats respectively. This effect of iodide did not depend on iodine organification and was not influenced by the changes of free amino acids pool. There were no significant differences in the relative concentration of 14C-labelled thyroglobulin and total 14C-thyroid protein. Differential fragility demonstrable by unfolding or dissociation was observed between different classes of thyroglobulin. The fragility was increasing from the old non-labelled molecules to newly iodinated and newly synthesized ones. It is concluded that iodide has a direct intrathyroidal blocking effect on thyroid protein synthesis which may contribute to its antigoitrogenic action. The lack of in vitro stimulation of protein synthesis by TSH remains unexplained.

Effect of Atrazine on Elongation of the Embryonic Axis of Red Kidney Bean

Weed Science ◽  
1974 ◽  
Vol 22 (3) ◽  
pp. 227-229 ◽  
Author(s):  
Parshall B. Bush ◽  
S. K. Ries
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Phaseolus Vulgaris ◽  
Embryonic Axis ◽  
Amino Acid Incorporation ◽  
Kidney Beans ◽  
Acid Incorporation ◽  
Red Kidney Bean ◽  
Red Kidney Beans ◽  
Stimulation Of

Atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-s-triazine] at a concentration of 10−8M stimulated the elongation of the embryonic axis of red kidney beans (Phaseolus vulgarisL. ‘Charlevoix’). This stimulation of elongation was accompanied by a light-independent increase in protein synthesis as measured by radioactive amino acid incorporation.

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