scholarly journals Gamma-ray-induced Changes in Plasma Membrane from Hypodermal Mesocarp Tissue of Muskmelon Fruit

HortScience ◽  
1995 ◽  
Vol 30 (4) ◽  
pp. 823E-823
Author(s):  
Gene E. Lester ◽  
Bruce D. Whitaker

Postharvest gamma-irradiation of melons at low dosage has been reported to extend shelf life. This study assessed how irradiation alters the structure and function of plasma membrane (PM) from hypodermal-mesocarp tissue. Administration of gamma rays (1 kGy at 0.017 kGy/min) to mature melon (Cucumis melo L.) fruit caused a 14% drop in H+-ATPase activity within 4 h. Total protein content did not differ in PM from non-irradiated (NIR) vs. irradiated (IR) fruits. Following storage (7 days at 7C then 3 days at 21C), H+-ATPase activity was ≈10% to 20% lower in PM from both groups of fruit, with no difference between the two. Total PM protein had declined by 34% and 49% in IR and NIR fruits, respectively. After irradiation, the phospholipid to protein ratio (PL:protein) was substantially higher in PM from IR fruit (0.67 vs. 0.58 in NIR). With storage, PL:protein dropped to 0.52 in NIR fruit PM, but changed little (0.65) in IR fruit PM. These results may indicate that irradiation stimulates PL synthesis or inhibits PL catabolism. Further analyses of PM lipid content and composition are underway.

1980 ◽  
Vol 85 (2) ◽  
pp. 213-227 ◽  
Author(s):  
J Beisson ◽  
J Cohen ◽  
M Lefort-Tran ◽  
M Pouphile ◽  
M Rossignol

Previous studies on exocytosis in Paramecium using mutants affecting trichocyst extrusion permitted us to analyze the assembly and function of three intramembrane particle arrays ("ring" and "rosette" in the plasma membrane, "annulus" in the trichocyst membrane) involved in the interaction between these two membranes. Using a conditional mutation, nd9, which blocks rosette assembly and prevents exocytosis at the nonpermissive temperature, we have analyzed the effect of temperature on the secretory capacity of nd9 cells. By combining several techniques (physiological studies, microinjections, inhibition of fatty acid synthesis, and freeze-fracture analysis) we demonstrate (a) that the product of the mutated allele nd9 is not thermolabile but that its activity is dependent upon temperature-induced changes in the membrane lipid composition and (b) that the product of the nd9 locus is a diffusible cytoplasmic component whose interaction with both plasma membrane and trichocyst membrane is required for rosette assembly and exocytosis. The data provide physiological evidence for the existence of a molecular complex(es) linking the two membranes and involved in the control of membrane fusion; we discuss the possible nature and function of these links.


2009 ◽  
Vol 59 (2) ◽  
pp. 125-135 ◽  
Author(s):  
Juan Carlos Alvarez-Pizarro ◽  
Enéas Gomes-Filho ◽  
Claudivan Feitosa de Lacerda ◽  
Nara Lídia Mendes Alencar ◽  
José Tarquínio Prisco

2013 ◽  
Vol 13 (1) ◽  
pp. 43-52 ◽  
Author(s):  
A. Brett Mason ◽  
Kenneth E. Allen ◽  
Carolyn W. Slayman

ABSTRACTThe C-terminal tail of yeast plasma membrane (PM) H+-ATPase extends approximately 38 amino acids beyond the final membrane-spanning segment (TM10) of the protein and is known to be required for successful trafficking, stability, and regulation of enzyme activity. To carry out a detailed functional survey of the entire length of the tail, we generated 15 stepwise truncation mutants. Eleven of them, lacking up to 30 amino acids from the extreme terminus, were able to support cell growth, even though there were detectable changes in plasma membrane expression, protein stability, and ATPase activity. Three functionally distinct regions of the C terminus could be defined. (i) Truncations upstream of Lys889, removing more than 30 amino acid residues, yielded no viable mutants, and conditional expression of such constructs supported the conclusion that the stretch from Ala881(at the end of TM10) to Gly888is required for stable folding and PM targeting. (ii) The stretch between Lys889and Lys916, a region known to be subject to kinase-mediated posttranslational modification, was shown here to be ubiquitinated in carbon-starved cells as part of cellular quality control and to be essential for normal ATPase folding and stability, as well as for autoinhibition of ATPase activity during glucose starvation. (iii) Finally, removal of even one or two residues (Glu917and Thr918) from the extreme C terminus led to visibly reduced expression of the ATPase at the plasma membrane. Thus, the C terminus is much more than a simple appendage and profoundly influences the structure, biogenesis, and function of the yeast H+-ATPase.


2014 ◽  
Vol 82 (2) ◽  
pp. 135-142 ◽  
Author(s):  
Mandeep Jeswan Singh ◽  
Jayani Chandrapala ◽  
Punsandani Udabage ◽  
Ian McKinnon ◽  
Mary Ann Augustin

The heat-induced changes in pH, Ca activity and viscosity after heating at 90 °C for 10 min of five modified skim milks were studied as a function of the initial pH of the milks at 25 °C. The milks had (i) different ratios of casein : whey protein (0·03, 1·74, 3·97, 5·27 and 7·25), (ii) the same total solids concentration (9% w/w) and (iii) prior to the adjustment of the pH, similar values of pH (6·67–6·74), concentration of serum calcium, and calcium activity, suggesting that the sera have similar mineral composition. The total protein concentrations of the milks differ (2·8–4·0%, w/w). The pH decrease in situ upon heating from 25–90 °C was similar for all the modified skim milks with the same starting pH, suggesting that the pH changes to milk on heating were primarily mediated by the initial mineral composition of the serum and were unaffected by the casein : whey protein ratio or the total protein content of the milk. The heat-induced changes in pH and calcium activity were largely reversible on cooling. The two milks with the lowest ratios of casein to whey protein gelled on heating to 90 °C for 10 min and cooling to 25 °C when the pH was adjusted to pH = 6·2 prior to heating. The viscosities of all other milks with casein to whey protein ratio of 3·97, 5·27 and 7·25 and/or pH ≥6·7 prior to heating did not change significantly. The effect of casein : whey protein ratio and the pH are the dominant factors in controlling the susceptibility to thickening of the milks on heating in this study.


1967 ◽  
Vol 31 ◽  
pp. 469-471
Author(s):  
J. G. Duthie ◽  
M. P. Savedoff ◽  
R. Cobb
Keyword(s):  

A source of gamma rays has been found at right ascension 20h15m, declination +35°, with an uncertainty of 6° in each coordinate. Its flux is (1·5 ± 0·8) x 10-4photons cm-2sec-1at 100 MeV. Possible identifications are reviewed, but no conclusion is reached. The mechanism producing the radiation is also uncertain.


1994 ◽  
Vol 144 ◽  
pp. 635-639
Author(s):  
J. Baláž ◽  
A. V. Dmitriev ◽  
M. A. Kovalevskaya ◽  
K. Kudela ◽  
S. N. Kuznetsov ◽  
...  

AbstractThe experiment SONG (SOlar Neutron and Gamma rays) for the low altitude satellite CORONAS-I is described. The instrument is capable to provide gamma-ray line and continuum detection in the energy range 0.1 – 100 MeV as well as detection of neutrons with energies above 30 MeV. As a by-product, the electrons in the range 11 – 108 MeV will be measured too. The pulse shape discrimination technique (PSD) is used.


Author(s):  
James Cronshaw ◽  
Jamison E. Gilder

Adenosine triphosphatase (ATPase) activity has been shown to be associated with numerous physiological processes in both plants and animal cells. Biochemical studies have shown that in higher plants ATPase activity is high in cell wall preparations and is associated with the plasma membrane, nuclei, mitochondria, chloroplasts and lysosomes. However, there have been only a few ATPase localization studies of higher plants at the electron microscope level. Poux (1967) demonstrated ATPase activity associated with most cellular organelles in the protoderm cells of Cucumis roots. Hall (1971) has demonstrated ATPase activity in root tip cells of Zea mays. There was high surface activity largely associated with the plasma membrane and plasmodesmata. ATPase activity was also demonstrated in mitochondria, dictyosomes, endoplasmic reticulum and plastids.


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