Ethylene Production by Subcellular Particles from Rat Liver, Rat Intestinal Mucosa and Penicillium Digitatum

Nature ◽  
1963 ◽  
Vol 197 (4865) ◽  
pp. 366-367 ◽  
Author(s):  
G. RAM CHANDRA ◽  
MARY SPENCER
1984 ◽  
Vol 259 (4) ◽  
pp. 2452-2456 ◽  
Author(s):  
M C Blaufuss ◽  
J I Gordon ◽  
G Schonfeld ◽  
A W Strauss ◽  
D H Alpers

1974 ◽  
Vol 140 (3) ◽  
pp. 549-556 ◽  
Author(s):  
R. L. Boeckx ◽  
K. Dakshinamurti

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.


1982 ◽  
Vol 201 (2) ◽  
pp. 405-410 ◽  
Author(s):  
J C Cameselle ◽  
M J Costas ◽  
M A G Sillero ◽  
A Sillero

The occurrence and distribution of bis-(5'-guanosyl) tetraphosphatase activity towards dinucleoside tetraphosphates between the 27 000 g supernatant and sedimented fraction were studied in liver, kidney, brain, muscle and intestinal mucosa from rat. The p1p4-bis-(5'-guanosyl) tetraphosphate-hydrolysing activities found in total homogenates were 0.77, 1.44, 0.39, 0.36 and 2.14 units (mumol/min)/g respectively. The activities found in the 27000 g-sedimented fractions were 74, 49, 11, 4 and 96% of those present in the homogenates respectively. The properties of the soluble enzymes were investigated. All of them have low Km values for p1p4-bis-(5'-guanosyl) tetraphosphate (from 2 to 50 microM), are competitively inhibited by guanosine 5'-tetraphosphate with K1 values from 10 to 160 nM, have molecular weights of about 21 000, require Mg2+ or Mn2+ and are inhibited by Ca2+. These properties show that bis-(5'-guanosyl) tetraphosphatase (EC 3.6.1.17), an enzyme previously characterized in Artemia salina and rat liver [Warner & Finamore (1965) Biochemistry 4, 1568-1575; Vallejo, Sillero & Sillero (1974) Biochim, Biophys. Acta 358, 117-125; Lobatón, Vallejo, Sillero & Sillero (1975) Eur. J. Biochem. 50, 495-501], is present in all the rat tissues examined. The inhibition of the enzyme by Ca2+ could be related to the effect of p1p4-bis-(5'-adenosyl) tetraphosphate as a trigger of DNA synthesis [Grummt, Waltl, Jantzen, Hamprecht, Huebscher & Kuenzle (1979) Proc. Natl. Acad. Sci. U.S.A. 76, 6081-6085].


1982 ◽  
Vol 31 (8) ◽  
pp. 1469-1474 ◽  
Author(s):  
Lida S. Morisoli ◽  
Aldo D. Mottino ◽  
JoséM. Pellegrino ◽  
Edgardo E. Guibert ◽  
Emilio A. Rodriguez Garay

1964 ◽  
Vol 23 (2) ◽  
pp. 233-240 ◽  
Author(s):  
Lichu Hsu ◽  
A. L. Tappel

Six intracellular hydrolases known to be associated with lysosomes in rat liver were found in rat intestinal mucosa. The extent to which they were particulate-bound and the degree of enzyme release when the particulate fractions were suspended in hypotonic media followed the same pattern in both mucosa and liver. The specific activities of the mucosa enzymes were either comparable to or slightly smaller than those of the liver enzymes. These results suggest that the mucosa hydrolases belong to lysosome-like particles. However, differential fractionation of the mucosa indicated that the particles from the mucosa sediment at lower centrifugal forces than do those from the liver and are more heterogeneous in size, bearing a closer resemblance to kidney lysosomes. Possible physiological functions of particulate-bound digestive enzymes in intestinal mucosa are discussed.


1979 ◽  
Vol 64 (1) ◽  
pp. 55-60 ◽  
Author(s):  
Autar K. Mattoo ◽  
Edo Chalutz ◽  
James D. Anderson ◽  
Morris Lieberman

2020 ◽  
Vol 6 (3) ◽  
pp. 175
Author(s):  
Ana-Rosa Ballester ◽  
Luis González-Candelas

Penicillium digitatum is the main fungal postharvest pathogen of citrus fruit under Mediterranean climate conditions. The role of ethylene in the P. digitatum–citrus fruit interaction is unclear and controversial. We analyzed the involvement of the 2-oxoglutarate-dependent ethylene-forming enzyme (EFE)-encoding gene (efeA) of P. digitatum on the pathogenicity of the fungus. The expression of P. digitatumefeA parallels ethylene production during growth on PDA medium, with maximum levels reached during sporulation. We generated ΔefeA knockout mutants in P. digitatum strain Pd1. These mutants showed no significant defect on mycelial growth or sporulation compared to the parental strain. However, the knockout mutants did not produce ethylene in vitro. Citrus pathogenicity assays showed no differences in virulence between the parental and ΔefeA knockout mutant strains, despite a lack of ethylene production by the knockout mutant throughout the infection process. This result suggests that ethylene plays no role in P. digitatum pathogenicity. Our results clearly show that EFE-mediated ethylene synthesis is the major ethylene synthesis pathway in the citrus postharvest pathogen P. digitatum during both in vitro growth on PDA medium and the infection process, and that this hormone is not necessary for establishing P. digitatum infection in citrus fruit. However, our results also indicate that ethylene produced by P. digitatum during sporulation on the fruit surface may influence the development of secondary fungal infections.


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