External enzymes of yeast: their nature and formation

Lampen, J. O.

doi:10.1007/bf02046409

Cited by 206 publications

(75 citation statements)

References 39 publications

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“…The material retained is thus made available for enzyme-organized or auto-organized assembly of the complete cell wall (NeEas & Svoboda, 1981). Liquid media, on the other hand, provide conditions only for formation of the fibrillar component (Eddy & Williamson, 1959;Kopecka et al, 1967), because they allow soluble glycoproteins to be released into the medium (Lampen, 1968;Svoboda & NeEas, 1970). The function of PEG during wall regeneration could be similar to that of gel media: the high viscosity of PEG and the number of hydrogen bonds formed between molecules make the diffusion of wall glycoproteins (mol.…”

Section: Discussionmentioning

confidence: 99%

Reversion of Yeast Protoplasts in Media containing Polyethylene Glycol

Svoboda

Piedra

1983

Microbiology

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Liquid medium supplemented with 35% (w/v) PEG supported regeneration of the cell wall in protoplasts of Saccharomyces cerevisiae. The regeneration was followed by reversion to normal cells. Both these morphogenetic processes were similar to those described previously in gelatin media. The frequency of reversion was estimated to be 20 to 30%. The regeneration medium with PEG also induced protoplast fusion, When complementary auxotrophs were used for fusion only the fused products proliferated, giving first regenerated protoplasts and then hybrid cells.

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Section: Discussionmentioning

confidence: 99%

Reversion of Yeast Protoplasts in Media containing Polyethylene Glycol

Svoboda

Piedra

1983

Microbiology

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“…form secreted into the periplasmic space and an apparently non-glycosylated form retained within the cell (Neumann & Lampen, 1967;Lampen, 1968). The glycosylated form has been used as a probe for the process of glycoprotein biosynthesis and secretion (Novick et al, 1981;Trimble et al, 1983;Esmon et al, 1987).…”

Section: Introductionmentioning

confidence: 99%

Regulation of invertase in Aspergillus nidulans: effect of different carbon sources

Vainstein¹,

Peberdy

1991

Microbiology

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Aspergillus nidulans produces an extracellular P-D-fructofuranoside fructohydrolase (invertase) when grown on a medium containing the P-fructofuranosides sucrose or raffinose, indicating that synthesis is subject to induction by the substrate. On a growth medium containing sucrose, production was maximal at 15 h in cultures incubated at 28 Co. After this time the level of detectable invertase in the cultures declined. A proportion of the enzyme was secreted during the linear growth phase of the fungus. Various sugars were investigated for induction of invertase, but only the two P-fructofuranosides induced high production levels; with the other sugars, the enzyme was produced only at a low constitutive level. Mycelium grown under repressive conditions (1% glucose), rapidly produced invertase when transferred to sucrose-containing medium. After 80 min the invertase level in these cultures was 26-fold higher than the constitutive level. The repressive effect of other sugars, e.g. glucose and xylose, on invertase production was also demonstrated in this experimental system.

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“…The release of some extracellular enzymes has been studied in Saccharomyces cerevisiae and its protoplasts, but this organism does not produce protease (Lampen, 1968). In Neurospora crassa (Matile, 1965;Matile, Jost & Moor, 1969, however, it has been shown that extracellular protease is located in lysosome-like cytoplasmic particles which are liberated to the exterior by a process of reverse pinocytosis.…”

Section: Introductionmentioning

confidence: 99%

Ammonium Repression of Extracellular Protease in Aspergillus nidulans

Cohen

1972

Journal of General Microbiology

110

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S U M M A R YExtracellular protease of Aspergillus nidulans is repressible by ammonium. A mutant (xprDI) selected for derepression of protease in the presence of ammonium is also derepressed for nitrate reductase, xanthine dehydrogenase and glutamate uptake; it retains the ability to use ammonium as sole nitrogen source. The mutant is partially dominant in heterozygous diploids. The mutation does not confer methylamine resistance, nor are methylamine-resistant (meaA) strains derepressed for protease.

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External enzymes of yeast: their nature and formation

Cited by 206 publications

References 39 publications

Reversion of Yeast Protoplasts in Media containing Polyethylene Glycol

Reversion of Yeast Protoplasts in Media containing Polyethylene Glycol

Regulation of invertase in Aspergillus nidulans: effect of different carbon sources

Ammonium Repression of Extracellular Protease in Aspergillus nidulans

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