Titlebook: Enzymes of Molecular Biology; Michael M. Burrell Book 1993 Humana Press 1993

avarice

Deoxyribonuclease I (EC 3.1.21.1) and II (EC 3.1.22.1),lar biology, The Type II restriction endonucleases obviously fall into this category, however they are a large subject on their own and therefore are dealt with in a separate section of this book. DNases acting preferentially on single-stranded DNA (ss DNA) substrates are also dealt with in another section of this chapter.

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cumulative

Outlook: Agile as the New Normal?,homononucleotides. This chapter focuses on the endoribonuclease RNase A (otherwise described as RNase, RNase I, or pancreatic ribonuclease), which shows some base specificity in where it cleaves RNA. The enzyme has been particularly well characterized at the molecular level.

雄辯

Agile in der Unternehmenspraxisused, for example, to reveal the protein components of cell organelles by the hydrolysis of tissue slices (.), and as an alternative to proteinase K to remove protein during plasmid DNA (.), chromosomal DNA (.), and RNA isolation (.–.). Another use of pronase is the production of a protein hydrolysate suitable for amino acid analysis (.,.).

fatty-acids

Agile eHealth Usability Evaluationely degrade double-stranded DNA (.–.). Mung-bean nuclease 1 is also reported to show a separate 3′-ω-monophosphatase activity (.) (..). Mung-bean nuclease 1 is a zinc metalloenzyme that requires Zn. and a reducing agent, such as cysteine, for both activity and stability.

現(xiàn)實(shí)

Mung-Bean Nuclease 1 (EC 3.1.30.1),ely degrade double-stranded DNA (.–.). Mung-bean nuclease 1 is also reported to show a separate 3′-ω-monophosphatase activity (.) (..). Mung-bean nuclease 1 is a zinc metalloenzyme that requires Zn. and a reducing agent, such as cysteine, for both activity and stability.

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