|
|
|
|
| LEADER |
00000cam a2200000 i 4500 |
| 001 |
SCIDIR_on1100588396 |
| 003 |
OCoLC |
| 005 |
20231120010351.0 |
| 006 |
m o d |
| 007 |
cr cnu---unuuu |
| 008 |
190509s2019 enk ob 000 0 eng d |
| 040 |
|
|
|a N$T
|b eng
|e rda
|e pn
|c N$T
|d N$T
|d EBLCP
|d OPELS
|d UKMGB
|d OCLCF
|d UKAHL
|d OCLCQ
|d CASUM
|d OCLCO
|d OCLCA
|d OCLCQ
|d UX1
|d VT2
|d OCLCA
|d NLW
|d OCLCO
|d OCLCQ
|d OCLCO
|d OCL
|d OCLCQ
|d OCLCO
|
| 015 |
|
|
|a GBB992187
|2 bnb
|
| 016 |
7 |
|
|a 019400244
|2 Uk
|
| 019 |
|
|
|a 1235844764
|
| 020 |
|
|
|a 9780128168301
|q (electronic bk.)
|
| 020 |
|
|
|a 0128168307
|q (electronic bk.)
|
| 020 |
|
|
|a 0128168293
|
| 020 |
|
|
|a 9780128168295
|
| 020 |
|
|
|z 9780128168295
|
| 035 |
|
|
|a (OCoLC)1100588396
|z (OCoLC)1235844764
|
| 050 |
|
4 |
|a QP671.F5
|
| 060 |
|
4 |
|a W1
|b ME9615K v.620 2019
|
| 060 |
|
4 |
|a QU 110
|
| 072 |
|
7 |
|a SCI
|x 008000
|2 bisacsh
|
| 072 |
|
7 |
|a PSD
|2 bicssc
|
| 082 |
0 |
4 |
|a 572/.7
|2 23
|
| 082 |
0 |
4 |
|a 574.19258
|2 23
|
| 100 |
1 |
|
|a Palfey, Bruce,
|e author.
|
| 245 |
1 |
0 |
|a New approaches for flavin catalysis /
|c Bruce A. Palfey.
|
| 264 |
|
1 |
|a London :
|b Academic Press,
|c 2019.
|
| 300 |
|
|
|a 1 online resource
|
| 336 |
|
|
|a text
|b txt
|2 rdacontent
|
| 337 |
|
|
|a computer
|b c
|2 rdamedia
|
| 338 |
|
|
|a online resource
|b cr
|2 rdacarrier
|
| 490 |
1 |
|
|a Methods in enzymology ;
|v volume 620
|
| 588 |
0 |
|
|a Online resource; title from PDF title page (EBSCO, viewed May 10, 2019)
|
| 505 |
0 |
|
|a Front Cover; New Approaches for Flavin Catalysis; Copyright; Contents; Contributors; Preface; Chapter One: Methods for determining the reduction potentials of flavin enzymes; 1. Introduction; 2. Spectroelectrochemistry method; 3. Xanthine oxidase method; 3.1. Materials; 3.2. Protocol; 3.3. Considerations; 3.4. Data analysis; 4. Effects of ligands; 5. Conclusion; References; Chapter Two: Anaerobic methods for the transient-state study of flavoproteins: The use of specialized glassware to define ... ; 1. Introduction; 1.1. O2 as a substrate or a reactive contaminant
|
| 505 |
8 |
|
|a 1.2. Categories of flavoprotein reactions2. Controlling the concentration of molecular oxygen; 2.1. The limits of anaerobiosis and approach with glove-boxes; 2.2. The advantages of specialized glassware; 2.3. Instrument design considerations; 2.4. The Schlenk line; 2.5. Anaerobic vessels: Tonometers and cuvettes; 2.6. Exchanging argon for dissolved dioxygen: Making a sample anaerobic; 2.7. Anaerobic preparation of the rapid-mixing instrument; 2.8. Method for mounting tonometers and syringes on the kinetic instrument; 2.9. Gas blending and sparging to control the dioxygen concentration
|
| 505 |
8 |
|
|a 3. Preparing reduced flavoproteins3.1. Titration with sodium hydrosulfite; 3.2. Double-mixing and reduction using the native reductant; 3.3. Enzymatic reduction using mediators; 3.4. Light mediated reduction; 4. Summary and conclusion; References; Chapter Three: Performing anaerobic stopped-flow spectrophotometry inside of an anaerobic chamber; 1. Introduction; 2. Anaerobic chambers; 2.1. Anaerobic chamber components; 2.2. Maintaining an anaerobic chamber; 2.2.1. Maintaining chamber anaerobiosis; 2.2.2. Maintaining humidity and removing hydrogen sulfide
|
| 505 |
8 |
|
|a 2.3. Flexible chambers compared to rigid chambers3. Introduction to stopped-flow spectrophotometry; 3.1. Components of a stopped-flow spectrophotometer; 3.2. Anaerobic stopped-flow spectrophotometry; 4. Setting up, preparing, and performing stopped-flow spectrophotometry assays inside of an anaerobic chamber; 4.1. Setting up a stopped-flow spectrophotometer inside of an anaerobic chamber; 4.1.1. Materials; 4.1.2. Procedure; 4.1.3. Notes; 4.2. Setting up a Schlenk line on a cart; 4.2.1. Equipment; 4.2.2. Procedure; 4.2.3. Notes; 4.3. Preparing anaerobic buffers; 4.3.1. Equipment
|
| 505 |
8 |
|
|a 4.3.2. Buffers and reagents4.3.3. Procedure; 4.3.4. Notes; 4.4. Transferring anaerobic solutions; 4.4.1. Equipment; 4.4.2. Procedure; 4.4.3. Notes; 4.5. Addition of enzymes to maintain anaerobic solutions; 4.5.1. Equipment; 4.5.2. Buffers or reagents; 4.5.3. Procedure; 4.5.4. Notes; 4.6. Determining oxygen concentration in deoxygenated buffers to validate anaerobiosis; 4.6.1. Equipment; 4.6.2. Buffers and reagents; 4.6.3. Procedure; 4.6.4. Notes; 4.7. Preparing anaerobic enzyme solutions; 4.7.1. Equipment; 4.7.2. Buffers and reagents; 4.7.3. Procedure; 4.7.4. Notes
|
| 504 |
|
|
|a Includes bibliographical references.
|
| 650 |
|
0 |
|a Flavins.
|
| 650 |
|
0 |
|a Flavoproteins.
|
| 650 |
|
0 |
|a Catalysis.
|
| 650 |
1 |
2 |
|a Flavins
|x chemistry
|0 (DNLM)D005415Q000737
|
| 650 |
2 |
2 |
|a Catalysis
|0 (DNLM)D002384
|
| 650 |
2 |
2 |
|a Flavoproteins
|x chemistry
|0 (DNLM)D005420Q000737
|
| 650 |
|
2 |
|a Flavins
|0 (DNLM)D005415
|
| 650 |
|
2 |
|a Flavoproteins
|0 (DNLM)D005420
|
| 650 |
|
6 |
|a Flavines.
|0 (CaQQLa)201-0026349
|
| 650 |
|
6 |
|a Flavoprot�eines.
|0 (CaQQLa)201-0026351
|
| 650 |
|
6 |
|a Catalyse.
|0 (CaQQLa)201-0025978
|
| 650 |
|
7 |
|a SCIENCE
|x Life Sciences
|x Biology.
|2 bisacsh
|
| 650 |
|
7 |
|a Catalysis
|2 fast
|0 (OCoLC)fst00848867
|
| 650 |
|
7 |
|a Flavins
|2 fast
|0 (OCoLC)fst00927097
|
| 650 |
|
7 |
|a Flavoproteins
|2 fast
|0 (OCoLC)fst00927107
|
| 655 |
|
4 |
|a Internet Resources.
|
| 830 |
|
0 |
|a Methods in enzymology ;
|v v. 620.
|
| 856 |
4 |
0 |
|u https://sciencedirect.uam.elogim.com/science/bookseries/00766879/620
|z Texto completo
|
