𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Enzymes of Molecular Biology Volume 16 || Pronase (EC 3.4.24.4)

✍ Scribed by Burrell, Michael M.


Book ID
120385920
Publisher
Humana Press
Year
1993
Tongue
English
Weight
965 KB
Category
Article
ISBN-13
9780896032347

No coin nor oath required. For personal study only.

✦ Synopsis


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. Nucleases: An Overview / A. Fred Weir -- Deoxyribonuclease I (ec 3.1.21.1) And Ii (ec 3.1.22.1) / A. Fred Weir -- Dna Polymerases (ec 2.7.7.7) / Martin J. Maunders -- Taq Polymerase (ec 2.7.7.7): With Particular Emphasis On Its Use In Pcr Protocols / Axel Landgraf And Heiner Wolfes -- Eukaryotic Nuclear Rna Polymerases (ec 2.7.7.6) / Deborah A. Cook And Robert J. Slater -- Reverse Transcriptase (ec 2.7.7.49): The Use Of Cloned Moloney Murine Leukemia Virus Reverse Transcriptase To Synthesize Dna From Rna / Gary F. Gerard And James M. D'alessio -- Terminal Deoxyribonucleotidyl Transferase (ec 2.7.7.31) / Frank Grosse And Andreas Manns -- Restriction Enzymes / Alfred Pingoud, Jurgen Alves And Robert Geiger -- Dna Methyltransferases (ec 2.1.1.72 And Ec 2.1.1.73) / David P. Hornby -- Dna And Rna Ligases (ec 6.5.1.1, Ec 6.5.1.2 And Ec 6.5.1.3) / Martin J. Maunders -- Bal 31 Nucleases (ec 3.1.11) / Horace B. Gray, Jr. And Tao Lu -- Mung-bean Nuclease 1 (ec 3.1.11) / Andrew J. Sharp And Robert J. Slater -- Rnase A (ec 3.1.27.5) / Michael M. Burrell -- Pronase (ec 3.4.24.4) / Patricia J. Sweeney And John M. Walker -- Proteolytic Enzymes For Peptide Production / Patricia J. Sweeney And John M. Walker -- Proteinase K (ec 3.4.21.14) / Patricia J. Sweeney And John M. Walker -- Carboxypeptidase Y (ec 3.4.16.1) / Julia S. Winder And John M. Walker -- Aminopeptidases: Aminopeptidase M (ec 3.4.11.2), Pyroglutamate Aminopeptidase (ec 3.4.19.3) And Prolidase (ec 3.4.13.9) / Patricia J. Sweeney And John M. Walker -- Alkaline Phosphatase (ec 3.1.3.1) / Martin J. Maunders -- Polynucleotide Kinase (ec 2.7.1.78) / Martin J. Maunders. Edited By Michael M. Burrell. Includes Bibliographical References And Index.


πŸ“œ SIMILAR VOLUMES


Comparative fine structural distribution
✍ JosΓ© Domingues Fontenele-Neto; Eduardo Ernst Massarelli; Paula Amaral Gurgel Gar πŸ“‚ Article πŸ“… 2001 πŸ› John Wiley and Sons 🌐 English βš– 873 KB

## Abstract Endopeptidase 24.15 (EP24.15) and 24.16 (EP24.16) are closely related metalloendopeptidases implicated in the metabolism of several neuropeptides and widely expressed in mammalian brain. To gain insight into the functional role of these two enzymes in the central nervous system, we exam

Novel roles of neuropeptide processing e
✍ S.I. Kim; V. Grum-Tokars; T.A. Swanson; E.J. Cotter; P.A. Cahill; J.L. Roberts; πŸ“‚ Article πŸ“… 2003 πŸ› John Wiley and Sons 🌐 English βš– 409 KB

## Abstract Neuropeptide processing metalloenzymes, such as angiotensin converting enzyme, neprilysin, endothelin converting enzyme, neurolysin, and EC3.4.24.15 (EP24.15), are central to the formation and degradation of bioactive peptides. We present EP24.15 as a paradigm for novel functions ascrib