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1.
Wien Klin Wochenschr Suppl ; 180: 34-8; discussion 57-9, 1990.
Artigo em Alemão | MEDLINE | ID: mdl-2321388

RESUMO

The concentrations of high molecular weight blood constituents are influenced by the increased intravascular pressure at sample collection. The impact on the fructosamine concentration was compared with that on total protein, plasma protein, electrolytes, and protein bound analytes such as calcium. The results show that fructosamine concentration behaves similar to that of total protein and albumin with change in resting position and venous-stasis.


Assuntos
Hexosaminas/sangue , Hipotensão Ortostática/sangue , Insuficiência Venosa/sangue , Adulto , Proteínas Sanguíneas/metabolismo , Cálcio/sangue , Permeabilidade Capilar/fisiologia , Feminino , Frutosamina , Humanos , Imunoglobulina G/metabolismo , Masculino , Albumina Sérica/metabolismo , Pressão Venosa/fisiologia
2.
Arch Microbiol ; 121(1): 91-6, 1979 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-223512

RESUMO

Inorganic phosphate inhibited the biosynthesis of the macrolide antibiotic turimycin in different strains of Streptomyces hygroscopicus. In the wild type strain a depression was observed with increasing phosphate concentrations. A total inhibition was found at 0.1 M phosphate. In a high producing mutant a minimum of turimycin production occured when the phosphate concentration was between 5 mM and 10 mM. Above this concentration the antibiotic synthesis increased again but the production period shifted to a later period of cultivation. Addition of inorganic phosphate resulted in an initial increase of intracellular cyclic AMP content. But a second elevation characterizing the normal level of cyclic AMP throughout the growth phase was prevented by phosphate. Exogenous cyclic AMP as well as positive effectors of the adenylyl cyclase system were able to overcome the phosphate suppression. Cyclic AMP abolished the reduction of protein synthesis following phosphate addition and caused the reappearance of a protein band which may be responsible for the turimycin biosynthesis.


Assuntos
Antibacterianos/biossíntese , AMP Cíclico/farmacologia , Fosfatos/farmacologia , Streptomyces/efeitos dos fármacos , Proteínas de Bactérias/biossíntese , AMP Cíclico/biossíntese , Glicosídeos/biossíntese , Lactonas/biossíntese , Mutação , Streptomyces/crescimento & desenvolvimento , Streptomyces/metabolismo
4.
Acta Otolaryngol ; 81(3-4): 315-22, 1976.
Artigo em Alemão | MEDLINE | ID: mdl-1266618

RESUMO

The gland-specific enzymes amylase, lysozyme and kallikrein the activities and their dependence on the speed of salivation were studied in normal persons. In these investigations the specification or standard ranges for differentiated secretion states is useful. In contrast to amylase activity, the activities of lysozyme and kallikrein weaken appreciably with increasing speed of salivation. The activity secreted, as measured in time units, increases. In the case of a diseased parotis, a comparison of enzyme activities with the standard values will show a significant reduction of lysozyme and amylase activity in the chronic processes. Acute inflammation affects the amylase activity slightly, but raises the lysozyme activity significantly. Parotid mixed tumours probably do not lead to any changes in the enzyme activities. The splitting up of amylase into isoenzymes by polyacrylamide gel electrophoresis and its possible importance for the diagnosis of pathological processes are discussed. First results of the splitting up of the parotid lysozyme are reported.


Assuntos
Amilases/metabolismo , Calicreínas/metabolismo , Muramidase/metabolismo , Glândula Parótida/enzimologia , Ensaios Enzimáticos Clínicos , Humanos , Glândula Parótida/fisiopatologia , Neoplasias Parotídeas/diagnóstico , Salivação
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