scholarly journals Effects of Progesterone on the Oestrogen-Stimulated Uterus: a Comparative Study of the Mouse, Guinea Pig, Rabbit and Sheep

1979 ◽  
Vol 32 (6) ◽  
pp. 549 ◽  
Author(s):  
BG Miller ◽  
Jennifer Wild ◽  
GM Stone
Keyword(s):  
Protein Synthesis ◽  
Guinea Pig ◽  
Comparative Study ◽  
Peroxidase Activity ◽  
Species Differences ◽  
Inhibitory Effects ◽  
Dna And Rna ◽  
Wet Weight ◽  
Vitro Protein

To examine more closely the anti-oestrogenic action of progesterone (P), its effect on various parameters in the 17 fl-oestradiol (E2)-primed uterus of the mouse, guinea pig, rabbit and ewe was studied. Changes in uterine wet weight, rate of in vitro protein synthesis, protein: DNA and RNA :. DNA ratios, peroxidase activity and the level of cytosol receptors for E2 and P were measured. Considerable between-species differences in the effect of P on these parameters were observed. The anti-uterotrophic action was greater in the mouse than in the guinea pig and was not seen in the rabbit or ewe. P inhibited protein synthesis in the mouse, was without significant effect in the guinea pig and was mildly stimulatory in the rabbit and ewe. Inhibitory effects on protein: DNA and RNA: DNA ratios were substantial in the mouse, minor in the guinea pig and absent in the rabbit and ewe. Peroxidase activity was decreased in the mouse and guinea pig, essentially lacking in the rabbit and not detectable in the ewe. In all species the level of both oestrogen and progesterone cytosol receptors was decreased, although the effect on the E2 receptor was less marked in the ewe.

scholarly journals Specific protein synthesis in isolated epithelium of guinea-pig seminal vesicle. Effects of castration and androgen replacement

1977 ◽  
Vol 166 (2) ◽  
pp. 167-173 ◽  
Author(s):  
Carlo M. Veneziale ◽  
John M. Burns ◽  
Jon C. Lewis ◽  
Kaspar A. Büchi
Keyword(s):  
Protein Synthesis ◽  
Guinea Pig ◽  
Protein Content ◽  
Seminal Vesicle ◽  
Specific Protein ◽  
Absolute Amount ◽  
Cytoplasmic Protein ◽  
Specific Proteins ◽  
Wet Weight

Four intrinsic soluble secretory proteins are synthesized in vitro by isolated seminal-vesicle mucosa from sexually mature guinea pigs. Newly synthesized specific proteins labelled with [14C]glycine and [14C]lysine were precipitated by using double-antibody immunoprecipitation techniques and their radioactivity was assessed. Rates of synthesis were determined on each of 5 days after castration. By 5 days after castration the wet weight of the epithelium decreased to 42% of intact control values; the absolute amount of specific protein synthesized in vitro after 60min incubation decreased to 28% and the 27500g cytoplasmic protein content decreased to 31%. Thus androgen deprivation leads to a decrease in general protein synthesis in vivo, as well as to a decrease in specific protein synthesis in vitro. Specific protein synthesis comprised 76% of the total protein formed in isolated tissue from animals 5 days after castration as compared with 99–100% in tissue from intact animals. At 72h after an injection of testosterone or dihydrotestosterone, seminal-vesicle epithelium wet weight, cytoplasmic protein content and capability for synthesizing specific proteins in vitro were restored to approx. 70% of normal values. At 72h after onset of therapy with 3α-androstanediol, both epithelium wet weight and cytoplasmic protein content had increased significantly, but without a corresponding increase in the capability of the isolated tissue to synthesize specific proteins. The soluble labelled proteins synthesized in vitro by isolated epithelium from intact animals during 60 or 120min incubation were essentially entirely immunoprecipitable, i.e. specific. In contrast, approx. 29% of all soluble protein newly synthesized by isolated epithelium from animals 5 days after castration was acid-precipitable, but not immunoprecipitable, i.e. ‘non-specific’. The injection of testosterone into castrated animals inhibited the synthesis of the non-specific fraction by isolated tissue. The effects of castration on the ultrastructure of guinea-pig seminal-vesicle epithelium are also presented.

Cell-free, protein-synthesizing system of photosynthetic and heterotrophic Rhodospirillum rubrum

1976 ◽  
Vol 22 (2) ◽  
pp. 304-308
Author(s):  
C. T. Chow
Keyword(s):  
Protein Synthesis ◽  
Protease Activity ◽  
Rhodospirillum Rubrum ◽  
Chemical Compounds ◽  
Protein Synthesis Inhibitors ◽  
Free Protein ◽  
Two Systems ◽  
The Difference ◽  
Vitro Protein

An active in vitro protein-synthesizing system has been developed from Rhodospirillum rubrum grown under either photosynthetic or heterotrophic conditions. A protease activity has been found in both of these systems, and this activity can be readily inactivated by treating the cells with KCl and phenylmethyl sulfonylfluoride. The difference in protein-synthesizing activity between the photosynthetic and the heterotrophic systems has been tested in regard to the requirement of various chemicals and the response to protein synthesis inhibitors or various chemical compounds. It has been concluded that only minor differences in protein-synthesizing activity exist between these two systems.

Use of an in Vitro Protein Synthesizing System to Test the Mode of Action of Chloracetamides

Weed Science ◽  
1980 ◽  
Vol 28 (3) ◽  
pp. 334-340 ◽  
Author(s):  
Luanne M. Deal ◽  
J. T. Reeves ◽  
B. A. Larkins ◽  
F. D. Hess
Keyword(s):  
Protein Synthesis ◽  
Sand Culture ◽  
Leucine Incorporation ◽  
Insoluble Protein ◽  
In Vitro System ◽  
A Cell ◽  
Protein Incorporation ◽  
Vitro Protein

The effects of chloracetamides on protein synthesis were studied both in vivo and in vitro. Four chloracetamide herbicides, alachlor [2-chloro-2′,6′-diethyl-N-(methoxymethyl)acetanilide], metolachlor [2-chloro-N-(2-ethyl-6-methylphenyl)-N-(2-methoxy-1-methylethyl)acetamide], CDAA (N–N-diallyl-2-chloroacetamide), and propachlor (2-chloro-N-isopropylacetanilide) were tested for inhibition of [3H]-leucine incorporation into protein. Incorporation of3H-leucine into trichloroacetic acid (TCA)-insoluble protein was inhibited in oat (Avena sativaL. ‘Victory’) seedlings grown in sand culture and treated 12 h at 1 × 10−4M with these chloracetamides. The herbicides were also tested in a cell-free protein synthesizing system containing polyribosomes purified from oat root cytoplasm. These herbicides had no effect on the rates of polypeptide elongation nor on the synthesis of specific polypeptides when herbicides (1 × 10−4M) were added directly to the system. Polypeptide formation was inhibited 89% when 1 × 10−4M cycloheximide was added during translation. Cytoplasmic polyribosomes were isolated from oat roots treated 12 h with 1 × 10−4M herbicide. Translation rates and products were not altered when these polyribosomes were added to the in vitro system. Protein synthesis is inhibited when tested in an in vivo system; however, the inhibition does not occur during the translation of mRNA into protein.

The effect of synthetic lysine and methionine on in vitro protein synthesis of weaning pigs

1995 ◽  
Vol 15 (3) ◽  
pp. 429-437 ◽  
Author(s):  
Y.M. Kwon ◽  
K.N. Heo ◽  
Y.J. Choi ◽  
I.K. Han ◽  
J.H. Woo
Keyword(s):  
Protein Synthesis ◽  
In Vitro Protein Synthesis ◽  
Weaning Pigs ◽  
Vitro Protein

[37] In vitro protein synthesis

1991 ◽  
pp. 536-545 ◽  
Author(s):  
Michael J. Leibowitz ◽  
Francis P. Barbone ◽  
Denise E. Georgopoulos
Keyword(s):  
Protein Synthesis ◽  
In Vitro Protein Synthesis ◽  
Vitro Protein
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