Structural requirements of choline derivatives for ‘conversion’ of pneumococcal amidase A new single‐step procedure for purification of this autolysin
- 23 May 1988
- journal article
- Published by Wiley in FEBS Letters
- Vol. 232 (2) , 308-312
- https://doi.org/10.1016/0014-5793(88)80759-2
Abstract
Tertiary amines appear to be the minimal structure needed to convert in vitro the inactive form (E‐form) of pneumococcal amidase to the catalytic active form (C‐form). Diethylethanolamine was one of the compounds that converted the E‐form, a finding that has been used successfully to develop an affinity chromatography system in DEAE‐cellulose for the rapid and efficient purification of lytic enzymes of pneumococcus and its bacteriophages.Keywords
This publication has 12 references indexed in Scilit:
- Molecular evolution of lytic enzymes of Streptococcus pneumoniae and its bacteriophages.Proceedings of the National Academy of Sciences, 1988
- Overproduction and rapid purification of the amidase of Streptococcus pneumoniaeArchiv für Mikrobiologie, 1987
- Biological role of the pneumococcal amidaseEuropean Journal of Biochemistry, 1987
- 3'-End modifications of the Streptococcus pneumoniae lytA gene: role of the carboxy terminus of the pneumococcal autolysin in the process of enzymatic activation (conversion)Gene, 1987
- Antibiotic Tolerance Among Clinical Isolates of BacteriaClinical Infectious Diseases, 1985
- Interaction of the pneumococcal amidase with lipoteichoic acid and cholineEuropean Journal of Biochemistry, 1985
- On the physiological functions of teichoic acidsJournal of Supramolecular Structure, 1975
- Abnormal Autolytic Enzyme in a Pneumococcus with Altered Teichoic Acid CompositionProceedings of the National Academy of Sciences, 1971