scholarly journals Quantitative Changes in In Vitro and In Vivo Protein Synthesis in Aging and Rejuvenated Soybean Cotyledons

1983 ◽  
Vol 71 (4) ◽  
pp. 861-868 ◽  
Author(s):  
Ronald W. Skadsen ◽  
Joe H. Cherry
1987 ◽  
Vol 127 (1) ◽  
pp. 413-426 ◽  
Author(s):  
A. J. EL HAJ ◽  
D. F. HOULIHAN

In vivo protein synthesis rates were measured in the carpopodite extensor muscle of the shore crab, Carcinus maenas, following a single, high-dose injection of [3H]phenylalanine, which stabilized specific radioactivities in the free pools. In intermoult animals the percentage of protein mass synthesized per day (the fractional rate of protein synthesis) was 1.15% day−1 for the whole extensor muscle. The small, slow-type tonic fibres in the extensor had fractional rates of protein synthesis some 2.1 times higher than those of the large, fast-type phasic fibres. Measurement of protein synthesis rates of extensor muscles from intermoult animals using an in vitro incubation over 2h gave fractional synthesis rates three times lower than those found in in vivo experiments. Compared with the intermoult animals, six- and three-fold increases in fractional synthesis rates were found in the extensor muscles from stages immediately preceding and following ecdysis, respectively. Microdissection of the muscle fibres revealed that the increased synthesis in postecdysial animals was occurring mainly at the external cuticular end of the muscle fibres. Autoradiographic analysis confirmed the cuticular end of the muscles as the major site of muscle protein synthesis. We conclude that the postecdysial increase in muscle fibre length and the associated increase in the sarcomere number is accompanied by an increase in protein synthesis in the muscles.


1984 ◽  
Vol 136 (2) ◽  
pp. 285-292 ◽  
Author(s):  
Thaddeus S. Nowak ◽  
Elizabeth R. Carty ◽  
W.David Lust ◽  
Janet V. Passonneau

1998 ◽  
Vol 22 ◽  
pp. 306-308
Author(s):  
M. D. Carro ◽  
E. L. Miller

The estimation of rumen microbial protein synthesis is one of the main points in the nitrogen (N)-rationing systems for ruminants, as microbial protein provides proportionately 0.4 to 0.9 of amino acids entering the small intestine in ruminants receiving conventional diets (Russell et al., 1992). Methods of estimating microbial protein synthesis rely on marker techniques in which a particular microbial constituent is related to the microbial N content. Marker : N values have generally been established in mixed bacteria isolated from the liquid fraction of rumen digesta and it has been assumed that the same relationship holds in the total population leaving the rumen (Merry and McAllan, 1983). However, several studies have demonstrated differences in composition between solid-associated (SAB) and fluid-associated bacteria in vivo (Legay-Carmier and Bauchart, 1989) and in vitro (Molina Alcaide et al, 1996), as well in marker : N values (Pérez et al., 1996). This problem could be more pronounced in the in vitro semi-continuous culture system RUSITEC, in which there are three well defined components (a free liquid phase, a liquid phase associated with the solid phase and a solid phase), each one having associated microbial populations.The objective of this experiment was to investigate the effect of using different bacterial isolates (BI) on the estimation of microbial production of four different diets in RUSITEC (Czerkawski and Breckenridge, 1977), using (15NH4)2 SO4 as microbial marker, and to assess what effects any differences would have on the comparison of microbial protein synthesis between diets.This study was conducted in conjunction with an in vitro experiment described by Carro and Miller (1997). Two 14-day incubation trials were carried out with the rumen simulation technique RUSITEC (Czerkawski and Breckenridge, 1977). The general incubation procedure was the one described by Czerkawski and Breckenridge (1977) and more details about the procedures of this experiment are given elsewhere (Carro and Miller, 1997).


2001 ◽  
Vol 20 (2) ◽  
pp. 181-182 ◽  
Author(s):  
A. JANUSZKIEWICZ ◽  
P. ESSÉN ◽  
M.A. McNURLAN ◽  
O. RINGDÉN ◽  
P.J. GARLICK ◽  
...  

2001 ◽  
Vol 268 (20) ◽  
pp. 5375-5385 ◽  
Author(s):  
Linda McKendrick ◽  
Simon J. Morley ◽  
Virginia M. Pain ◽  
Rosemary Jagus ◽  
Bhavesh Joshi

1975 ◽  
Vol 146 (3) ◽  
pp. 675-685 ◽  
Author(s):  
S G Siddell ◽  
R J Ellis

The function of plastid ribosomes in pea (Pisum sativum L.) was investigated by characterizing the products of protein synthesis in vitro in plastids isolated at different stages during the transition from etioplast to chloroplast. Etioplasts and plastids isolated after 24, 48 and 96h of greening in continuous white light, use added ATP to incorporate labelled amino acids into protein. Plastids isolated from greening leaves can also use light as the source of energy for protein synthesis. The labelled polypeptides synthesized in isolated plastids were analysed by electrophoresis in sodium dodecyl sulphate-ureapolyacrylamide gels. Six polypeptides are synthesized in etioplasts with ATP as energy source. Only one of these polypeptides is present in a 150 000g supernatant fraction. This polypeptide has been identified as the large subunit of Fraction I protein (3-phospho-D-glycerate carboxylyase EC 4.1.1.39) by comparing the tryptic ‘map’ of its L-(35S)methionine-labelled peptides with the tryptic ‘map’ of large subunit peptides from Fraction I labelled with L-(35S)methionine in vivo. The same gel pattern of six polypeptides is seen when plastids isolated from greening leaves are incubated with either added ATP or light as the energy source. However, the rates of synthesis of particular polypeptides are different in plastids isolated at different stages of the etioplast to chloroplast transition. The results support the idea that plastid ribosomes synthesize only a small number of proteins, and that the number and molecular weight of these proteins does not alter during the formation of chloroplasts from etioplasts.


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