Library Science

Provides key information on a wide range of enzymes commonly used as tools in molecular biology, helping to minimize the time a scientist spends researching the literature to get reactions to work efficiently and allowing the nonenzymologist to design an experiment. Each chapter gives background information on the enzyme selected and those parameters important in its use, describes both the source and application of the enzyme, and provides details on the size and structure of the protein. Specific parameters essential for achieving an optimized reaction are discussed, along with exemplary practical procedures an protocols.

Authors: Burrell, Michael M.

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Table of Contents

1. Nucleases: An Overview (pp. 1-6)
   Weir, A. Fred
2. Deoxyribonuclease I (EC 3.1.21.1) and II (EC 3.1.22.1) (pp. 7-16)
   Weir, A. Fred
3. DNA Polymerases (EC 2.7.7.7) (pp. 17-30)
   Maunders, Martin J.
4. Taq Polymerase (EC 2.7.7.7): With Particular Emphasis on Its Use in PCR Protocols (pp. 31-58)
   Landgraf, Axel; Wolfes, Heiner
5. Eukaryotic Nuclear RNA Polymerases (EC 2.7.7.6) (pp. 59-72)
   Cook, Deborah A.; Slater, Robert J.
6. Reverse Transcriptase (EC 2.7.7.49): The Use of Cloned Maloney Murine Leukemia Virus Reverse Transcriptase to Synthesize DNA from RNA (pp. 73-94)
   Gerard, Gary E; D???Alessio, James M.
7. Terminal Deoxyribonucleotidyl Transferase (EC 2.7.7.31) (pp. 95-106)
   Grosse, Frank; Manns, Andreas
8. Restriction Enzymes (pp. 107-200)
   Pingoud, Alfred; Alves, Jurgen; Geiger, Robert
9. DNA Methyltransferases (EC 2.1.1.72 and EC 2.1.1.73) (pp. 201-212)
   Hornby, David P.
10. DNA and RNA Ligases (EC 6.5.1.1, EC 6.5.1.2, and EC 6.5.1.3) (pp. 213-230)
    Maunders, Martin J.
11. The BAL 31 Nucleases (EC 3.1.11) (pp. 231-252)
    Gray, Horace B.; Lu, Tao
12. Mung-Bean Nuclease 1 (EC 3.1.30.1) (pp. 253-262)
    Sharp, Andrew J.; Slater, Robert J.
13. RNase A (EC 3.1.27.5) (pp. 263-270)
    Burrell, Michael M.
14. Pronase (EC 3.4.24.4) (pp. 271-276)
    Sweeney, Patricia J.; Walker, John M.
15. Proteolytic Enzymes for Peptide Production (pp. 277-304)
    Sweeney, Patricia J.; Walker, John M.
16. Proteinase K (EC 3.4.21.14) (pp. 305-312)
    Sweeney, Patricia J.; Walker, John M.
17. Carboxypeptidase Y (EC 3.4.16.1) (pp. 313-318)
    Winder, Julia S.; Walker, John M.
18. Aminopeptidases: Aminopeptidase M (EC 3.4.11.2), Pyroglutamate Aminopeptidase (EC 3.4.19.3), and Prolidase (EC 3.4.13.9) (pp. 319-330)
    Sweeney, Patricia J.; Walker, John M.
19. Alkaline Phosphatase (EC 3.1.3.1) (pp. 331-342)
    Maunders, Martin J.
20. Polynucleotide Kinase (EC 2.7.1.78) (pp. 343-356)
    Maunders, Martin J.

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