Esterase. VIII. Histochemische, elektrophoretische und quantitative Untersuchungen zum Einfluß von Phenobarbital auf die Leberesterase der Maus

Staeudinger, M.; Deimling, Otto von; Grossarth, C; Wienker, T. F.

doi:10.1007/bf00303983

Cited by 26 publications

(3 citation statements)

References 23 publications

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“…Lipase activity was measured in 200-ll aliquots of sonicated cells or of culture supernatants in 1 ml of 0.1 M sodium phosphate buer pH 7.4, using p-nitrophenyl caprylate as a substrate (StaÈ udinger et al 1973). The reaction was followed spectrophotometrically for 3 min at 410 nm.…”

Section: Lipase Assaymentioning

confidence: 99%

Specificity of the lipase-specific foldases of gram-negative bacteria and the role of the membrane anchor

et al. 1999

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Folding of lipases that are secreted by Pseudomonads and other gram-negative bacteria via the type II secretion pathway is facilitated by dedicated chaperones, called lipase-specific foldases (Lifs). Lifs are membrane-anchored proteins with a large periplasmic domain. The functional interaction between the Lif and its cognate lipase is specific, since the Pseudomonas aeruginosa Lif was found not to substitute for Lifs from Burkholderia glumae or Acinetobacter calcoaceticus. However, the P. aeruginosa Lif was able to activate the lipase from the closely related species P. alcaligenes. Hybrid proteins constructed from parts of the P. aeruginosa and B. glumae Lifs revealed that the C-terminal 138 amino acids of the B. glumae Lif determine the specificity of the interaction with the cognate lipase. Furthermore, the periplasmic domain of the B. glumae Lif was functional when cloned in frame with a cleavable signal sequence, which demonstrates that the membrane anchor is not essential for Lif function in vivo. However, the recombinant Lif was released into the medium, indicating that the function of the membrane anchor is to prevent secretion of the Lif together with the lipase.

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Section: Lipase Assaymentioning

confidence: 99%

Specificity of the lipase-specific foldases of gram-negative bacteria and the role of the membrane anchor

et al. 1999

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“…DNase production was measured qualitatively by the metachromatic agar diffusion method of Lachica et al (16) and quantitatively in units of nuclease activity per milligram of staphylococcal protein by the method of Heins et al (9). Quantitative lipase activity in micromoles of nitrophenyl released per minute per milliliter of staphylococcal supernatants was determined by the method of Staeudinger et al (26). Casein proteolysis was determined after 48 h of incubation in 10% CO2 on yeast extractsodium caseinate medium as described by Martley et al (17).…”

Section: Methodsmentioning

confidence: 99%

Phenotypic distinctiveness of Staphylococcus aureus strains associated with toxic shock syndrome

Todd¹,

Franco-Buff²,

Lawellin³

et al. 1984

Infect Immun

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Twenty Staphylococcus aureus strains from patients with toxic shock syndrome (TSS) and 20 from control patients (non-TSS) with infection but no clinical evidence of TSS were compared phenotypically in a collaborative, blinded, randomized study. TSS strains were significantly (P less than 0.05) more likely than non-TSS strains to produce various previously described but related toxic shock-associated proteins (pyrogenic exotoxin C, enterotoxin F, and TSS marker protein), as well as differing in other distinctive phenotypic characteristics, such as hemolysis, bacteriocin susceptibility, arsenate resistance, pigment production, and casein proteolysis. TSS strains were significantly less likely to carry plasmids than control strains. A combination of two variables--proteolysis and toxic shock-associated protein production--statistically accounted for all other phenotypic variations between TSS and non-TSS strains. Only proteolysis covaried with all other significant variables, suggesting a primary role in the phenotypic distinctiveness of TSS S. aureus strains and possibly in the pathogenesis of TSS.

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“…After centrifugation at 100 000 g the esterase activity was measured with p-nitrophenyl propionate (4 NP-O-3) as described previously (Huggins Se Lapides 1947;Staeudinger et al 1973). After centrifugation at 100 000 g the esterase activity was measured with p-nitrophenyl propionate (4 NP-O-3) as described previously (Huggins Se Lapides 1947;Staeudinger et al 1973).…”

Section: Enzyme Assay and Electrophoresismentioning

confidence: 99%

Esterase XXV

Deimling

Riebschläger

1977

Acta Endocrinologica

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The Es-9 esterase is expressed in the cortical zone of the NMRI mouse kidney only in the presence of testosterone. In disc electrophoresis, three esterase bands, absent in the control, emerge under the influence of exogenous testosterone, accompanied by the appearance of active sites, as shown by marking with [3H]diisopropyl fluorophosphate ([3H]DFP). It is suggested that the testosterone dependent appearance of Es-9 activity is due to true enzyme induction which requires the presence of an intact testosterone receptor.

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Esterase. VIII. Histochemische, elektrophoretische und quantitative Untersuchungen zum Einfluß von Phenobarbital auf die Leberesterase der Maus

Cited by 26 publications

References 23 publications

Specificity of the lipase-specific foldases of gram-negative bacteria and the role of the membrane anchor

Specificity of the lipase-specific foldases of gram-negative bacteria and the role of the membrane anchor

Phenotypic distinctiveness of Staphylococcus aureus strains associated with toxic shock syndrome

Esterase XXV

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