Summary
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1.
Treatment of Streptomyces albus G with lysozyme (mg dry weight mycelium/mg lysozyme = 2–3/1) leads to the isolation of membrane fractions whose yields amount to 12–20% of the total celullar protein depending upon the age and state of the bacterial culture.
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2.
The isolated fractions are composed of 52.7 per cent protein and 41 per cent lipid with minor amounts of hexose (2.3–2.4%), hexosamines (1.6–2.1%), RNA (2%) and DNA (0.45%). They possess a chemical composition similar to that of other membrane systems.
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3.
NADH oxidase activities are associated with the membrane fractions from cells of 18–20 h of age. These activities are not detected in the membrane fractions from older cells.
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4.
All membrane fractions shape small vesicles. Differences in size and shape are, however, found between membrane preparations from cells of distinct ages.
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5.
dd-carboxypeptidase is not selectively localized in a membrane fraction of a certain age. The subcellular distribution of this activity is similar to that of other lytic endopeptidases of S. albus G.
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6.
The amounts of dd-carboxypeptidase associated with the various membrane fractions are variable and never very high. The specificity of the dd-carboxypeptidase activity associated with membrane fractions differs from that of the soluble enzyme.
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7.
These results are discussed in relationship with the carboxypeptidase-transpeptidase hypothesis (Leyh-Bouille et al., 1970).
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Abbreviations
- DCIP:
-
2,6-dichlorophenol-indophenol
- SA endopeptidase:
-
a lytic endopeptidase which lyses Staphylococcus aureus cell walls liberating NH2 groups of glycine: F1 or “32” enzymes: endo-N-acetyl-muramyl glycan hydrolases from Streptomyces albus G
- Dap:
-
diaminopimelic acid
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Muñoz, E., Marquet, A., Larraga, V. et al. Isolation, partial characterization of the cytoplasmic membrane fraction of Streptomyces albus G and dd-carboxypeptidase localization. Archiv. Mikrobiol. 81, 273–288 (1972). https://doi.org/10.1007/BF00412246
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DOI: https://doi.org/10.1007/BF00412246