Specificity of the Autolysin of Streptococcus ( Diplococcus ) pneumoniae

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Specificity of the autolysin of Streptococcus (Diplococcus) pneumoniae.

A Streptococcus (Diplococcus) pneumoniae autolysin, partially purified from cellular autolysates, was optimally active at pH 7.0 and was stimulated by monovalent cations. Addition of autolysin to walls resulted in the appearance of only N-terminal l-alanine, whereas no glycosidase activity was observed. Walls which had been solubilized by autolysin were separated by gel filtration into a low-mo...

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Cloning of Minor Autolysin of Streptococcus Pneumoniae

Abstract Background and Objective: Increased antibiotic resistant strains and inadequacy of current vaccines against pneumococcal infections necessitate the study of novel protein antigens. It seems that minor autolysin of Streptococcus pneumoniae may have antigenicity. Thus, we aimed at cloning its gene for the first time. Material and Methods: After DNA extraction of Streptococcus pneumoniae ...

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Five of the six known glycosidases in the culture medium of Streptococcus pneumoniae have been purified from 600to 55,000-fold by a systematic procedure of ion exchange and affinity chromatography. Following partial separation of the glycosidases on DEAE-Sephadex, the neuraminidase, the endo-cu-N-acetylgalactosaminidase, the /3-galactosidase, and the P-iV-acetylglucosaminidase were further puri...

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The Fine Structure of Diplococcus Pneumoniae

The fine structure of an unencapsulated strain of Diplococcus pneumoniae is described. A striking feature of these bacteria is an intracytoplasmic membrane system which appears to be an extension of septa of dividing bacteria. The possible function of these structures and their relationship to the plasma membrane and other types of intracytoplasmic membranes found in pneumococcus is discussed.

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autolytic activity and plasma binding study of aap, a novel minor autolysin of streptococcus pneumoniae

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ژورنال

عنوان ژورنال: Journal of Bacteriology

سال: 1974

ISSN: 0021-9193,1098-5530

DOI: 10.1128/jb.117.2.796-804.1974