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在色谱分析、有机合成和交叉偶联反应领域已被 1 篇同行评审文献引用。
Characteristics of Micrococcal Nuclease from S. aureus:
Exhibits both exo- and endo-5'-phosphodiesterase activities against both DNA and RNA (Alexander et al. 1961). The enzyme catalyzes preferential endohydrolysis of the RNA and DNA at sites rich in adenylate or uridylate and deoxyadenylate or thymidylate (Roberts et al. 1962; Rushisky et al. 1962).
The amino acid sequence has been reported by Cone et al. (1971). The active site has been reported on by Chaiken and Anfinsen (1971), Cuatrecasas (1970), and Cuatrecasas et al. (1968). See also: Furie et al. 1973), Bonhert and Taniuchi (1972), Sacks et al. (1972), Arnone et al. (1971), Epstein et al. (1971), Chaiken and Anfinsen (1970), Cohen et al. (1970), Markley et al. (1970), Putter et al. (1970), and Schechter et al. (1970).
16,807 (Taniuchi et al. 1967b).
The pH optimum is reported as 9.2. However, the enzymic activity has an absolute requirement for Ca2+ and the pH optimum varies according to Ca2+ concentration (Heins et al. 1967).
= 9.2 (Fuchs et al. 1967).
5'-dioxynucleotides and 5'-ribonucleotides are inhibitory with the former demonstrating greatest inhibition.
Ca2+ is essential for activity. (See, however, Frank et al. 1975). Both RNase and DNase activities are competitively inhibited by deoxythymidine 3',5' diphosphate (Cuatrecasas et al. 1967). Sulkowski and Laskowski, Sr. (1970) indicate that the kinetics of degradation of RNA and DNA differ. They found no activation with Sr2+. See also: Dunn et al. (1973), Rammler et al. (1972), Chaiken and Anfinsen (1971), Markley and Jardetzy (1970) and Mikulski et al. (1969).