Abstract
NAD+-glycohydrolase from Streptococcus pyogenes was purified by successive chromatography on CM Sepharose CL-6B, Sephacryl S-200 HR and hydroxyapatite. The purified enzyme possessed synthesis and hydrolysis activities of cyclic ADP-ribose (cADPR), a newly found second messenger for Ca2+ mobilisation, along with cleavage activity of the ribose-nicotinamide bond in NAD+.
Original language | English |
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Pages (from-to) | 201-204 |
Number of pages | 4 |
Journal | FEMS Microbiology Letters |
Volume | 130 |
Issue number | 2-3 |
DOIs | |
Publication status | Published - 1995 Aug 1 |
Keywords
- ADP-ribosyl cyclase
- Cyclic ADP-ribose
- Cyclic ADP-ribose hydrolase
- NAD-glycohydrolase
- Streptococcus pyogenes
ASJC Scopus subject areas
- Microbiology
- Molecular Biology
- Genetics