Eine Mikromethode zur schnellen und spezifischen Serienbestimmung des Proteingehaltes unzerstörter Mikroorganismen

Hesse, Gerhard; Lindner, Robert; Müller, Rita

doi:10.1002/jobm.3630110703

Z Allg Mikrobiol

1971

DOI: 10.1002/jobm.3630110703

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Eine Mikromethode zur schnellen und spezifischen Serienbestimmung des Proteingehaltes unzerstörter Mikroorganismen

Gerhard Hesse¹,

Robert Lindner²,

Rita Müller³

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1975

1985

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Cited by 29 publications

References 6 publications

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Bestimmung des isoelektrisch fällbaren Proteins aufgeschlossener Mikroorganismen mittels Coomassiebrillantblau G‐250

Pauli¹,

Kreuter²

1985

Acta Biotechnologica

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An analytical method for a rapid determination of the protein dissolved from microorganisms after cell disintegration and protein extraction is presented, thereby distinguishing both the isoelectrical precipitable and the isoelectrical nonprecipitable protein fraction. The method is especially usefull for controlling disintegration and protein extraction steps in production of protein isolates from microbial biomasses.

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Bestimmung des isoelektrisch fällbaren Proteins aufgeschlossener Mikroorganismen mittels Coomassiebrillantblau G‐250

Pauli¹,

Kreuter²

1985

Acta Biotechnologica

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Alkoholdehydrogenase (ADH) in Hefezellen I. Grundplasmatische, mitochondriale und nucleäre ADH in Saccharomyces carlsbergensis und Kluyveromyces fragilis

Künkel¹,

May²

1976

J of Basic Microbiology

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When grown in a medium containing lactat, Saccharomyces carlsbergensis produces 5 times more ground‐plasmatic ADH than Kluyveromyces fragilis. Upon gelelectrophoresis, K. fragilis exhibits 7 bands while S. carlsbergensis shows only one. In a polyacrylamid gradient, the ADH's of both strains yield one band, the position of which corresponds to a molecular weight of about 160 000 D. In cell homogenates and mitochondrial fractions of S. carlsbergensis treated with ultrasound, an ADH is detected which exhibits 3 subbands and a molecular weight greater than 1 Megadalton. This ADH does not occur in K. fragilis. Mitochondrial fractions from K. fragilis contain an ADH, the electrophoretical mobility of which is identical to that of the ADH of the groundplasma. Nuclei of S. carlsbergensis also possess ADH whereas those of K. fragilis probably do not.

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Steroidumwandelnde Enzyme aus Mikroorganismen. XIII. Beziehungen zwischen Steroidstruktur und Induktion der 4‐En‐3‐oxosteroid: (Akzeptor)‐l‐en‐oxidoreduktase in Nocardia opaca

Hörhold

Hüller

Rose

1980

J of Basic Microbiology

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The induction of the 4-ene-3-oxosteroid: (acceptor)-1-ene-oxidoreductase in Nocardia opaca has been shown to be dependent on both hydrophilic and hydrophobic structural features of the steroid molecule, i.g. the nature of the oxygen function in positions 11 and 20 and the presence of the methyl group in position 10 influence the induction of the enzyme drastically. In this connection the metabolism of the steroid inductors being degradated during the induction process has been considered.

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Eine Mikromethode zur schnellen und spezifischen Serienbestimmung des Proteingehaltes unzerstörter Mikroorganismen

Cited by 29 publications

References 6 publications

Bestimmung des isoelektrisch fällbaren Proteins aufgeschlossener Mikroorganismen mittels Coomassiebrillantblau G‐250

Bestimmung des isoelektrisch fällbaren Proteins aufgeschlossener Mikroorganismen mittels Coomassiebrillantblau G‐250

Alkoholdehydrogenase (ADH) in Hefezellen I. Grundplasmatische, mitochondriale und nucleäre ADH in Saccharomyces carlsbergensis und Kluyveromyces fragilis

Steroidumwandelnde Enzyme aus Mikroorganismen. XIII. Beziehungen zwischen Steroidstruktur und Induktion der 4‐En‐3‐oxosteroid: (Akzeptor)‐l‐en‐oxidoreduktase in Nocardia opaca

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