Secure CheckoutPersonal information is secured with SSL technology.
Free ShippingFree global shipping
No minimum order.
Hydrocarbons and Related Compounds: Enzymes of Alkane and Alkene Utilization:
S.W. May and A.G. Katopodis, Hydrocarbon Monooxygenase System of Pseudomonas oleovorans.
W.R. Finnerty, Assay Methods for Long-Chain Alkane Oxidation in Acinetobacter.
W.R. Finnerty, Primary Alcohol Dehydrogenases from Acinetobacter.
W.R. Finnerty, Aldehyde Dehydrogenases from Acinetobacter.
W. Ashraf and J.C. Murrell, Propane-Specific Alcohol Dehydrogenase from Rhodococcus rhodochrous PNKb1.
J.C. Murrell and W. Ashraf, Cell-Free Assay Methods for Enzymes of Propane Utilization.
B.W. Groen and J.A. Duine, Quinoprotein Alcohol Dehydrogenase from Pseudomonas aeruginosa and Quinhemoprotein Alcohol Dehydrogenase from Comamonas testosteroni (Pseudomonas testosteroni).
Enzymes Involved in Cyclic and Aromatic Hydrocarbon Utilization:
L.P. Wackett, Toluene Dioxygenase from Pseudomonas putida F1.
B.D. Ensley and B.E. Haigler, Naphthalene Dioxygenase from Pseudomonas NCIB 9816.
P.J. Geary, J.R. Mason, and C.L. Joannou, Benzene Dioxygenase from Pseudomonas putida ML2 (NCIB 12190).
C.J. Batie and D.P. Ballou, Phthalate Dioxygenase.
P.W. Trudgill, Cyclohexanone 1,2-Monooxygenase from Acinetobacter NCIMB 9871.
P.W. Trudgill, Cyclohexanone 1,2-Monooxygenase from Pseudomonas NCIMB 9872.
J.W. Whittaker, A.M. Orville, and J.D. Lipscomb, Protocatechuate 3,4-Dioxygenase from Brevibacterium fuscum.
D.M. Arciero, A.M. Orville, and J.D. Lipscomb, Protocatechuate 4,5-Dioxygenase from Pseudomonas testosteroni.
S.A. Wolgel, and J.D. Lipscomb, Protocatechuate 2,3-Dioxygenase from Bacillus macerans.
M.R. Harpel and J.D. Lipscomb, Gentisate 1,2-Dioxygenase from Pseudomonas acidovorans.
A.M. Orville, M.R. Harpel, and J.D. Lipscomb, Synthesis of 17O- or 18O-Enriched Dihydroxy Aromatic Acids.
I.A. Kataeva and L.A. Golovleva, Catechol 2,3-Dioxygenases from Pseudomonas aeruginosa 2X.
K.-L. Ngai, E.L. Neidle, and L.N. Ornston, Catechol and Chlorocatechol 1,2-Dioxygenases.
R.B. Meagher, K.-L. Ngai, and L.N. Ornston, Muconate Cycloisomerase.
R.B. Meagher, K.-L. Ngai, and L.N. Ornston, Muconolactone Isomerase.
J.R. Mason and P.J. Geary, cis-1,2-Dihydroxycyclohexa-3,5-diene (NAD) Oxidoreductase (cis-Benzene Dihydrodiol Dehydrogenase) from Pseudomonas putida.
B. Entsch, Hydroxybenzoate Monooxygenase.
C.E. Cerniglia and M.A. Heitkamp, Polycyclic Aromatic Hydrocarbon Degradation by Mycobacterium.
J. Gibson, J. Geissler, and C.S. Harwood, Benzoate-CoA Ligase from Rhodopseudomonas palustris.
Yeast and Fungal Enzymes of Hydrocarbon Degradation:
K. Kirk, M. Tien, P.J. Kersten, B. Kalyanaraman, K.E. Hammell, and R.L. Farrell, Lignin Peroxidase from Fungi: Phanerochaeti chrysosporium.
M. Ueda and A. Tanaka, Long-Chain Alcohol Dehydrogenase of Candida Yeast.
Methylotrophy: Dissimilatory Enzymes of Methylotrophic Bacteria:
S.J. Pilkington and H. Dalton, Soluble Methane Monooxygenase from Methylococcus capsulatus Bath.
B.G. Fox, W.A. Froland, D.R. Jollie, and J.D. Lipscomb, Methane Monooxygenase from Methylosinus trichosporium OB3b.
J. Frank and J.A. Duine, Methanol Dehydrogenase from Hyphomicrobium X.
D. Day and C. Anthony, Methanol Dehydrogenase from Methylobacterium extorquens AM1.
A.R. Long and C. Anthony, Modifier Protein for Methanol Dehydrogenase of Methylotrophs.
N. Arfman and L. Dijkhuizen, Methanol Dehydrogenase from Thermotolerant Methylotroph Bacillus C1.
W.S. McIntire, Mathylamine Oxidase from Arthrobacter P1.
J.E. van Wielink, J. Frank, and J.A. Duine, Methylamine Dehydrogenase from Thiobacillus versutus.
V.L. Davidson, Methylamine Dehydrogenases from Methylotrophs.
M.Y. Kiriukhin, A.Y. Chistoserdov, and Y.D. Tsygankov, Methylamine Dehydrogenase from Methylobacillus flagellatum.
W.S. McIntire, Trimethylamine Dehydrogenase from Bacterium W3A1.
R.A. van der Meer, B.W. Groen, M.A.G. van Kleef, J. Frank, J.A. Jongejan, and J.A. Duine, Isolation, Preparation, and Assay of Pyrroloquinoline Quinone.
C. Anthony, Blue Copper Proteins Involved in Methanol and Methylamine Oxidation.
A.A. DiSpirito, Soluble Cytochromes c from Methylomonas A4.
D. Day and C. Anthony, Soluble Cytochromes c of Methanol-Utilizing Bacteria.
J. Frank and J. Duine, Cytochrome cL and Cytochrome cH from Hyphomicrobium X.
M. Husain, Electron-Transfer Flavoprotein from Methylophilus methylotrophus and Bacterium W3A1.
M.M. Attwood, Formaldehyde Dehydrogenases from Methylotrophs.
J.A. Duine, NAD-Linked, Factor-Independent and Glutathione-Independent Aldehyde Dehydrogenase from Hyphomicrobium X.
D.R. Jollie and J.D. Lipscomb, Formate Dehydrogenase from Methylosinus trichosporium OB3b.
L.V. Kletsova, M.Y. Kiriukhin, A.Y. Chistoserdov, and Y.D. Tsygankov, Glucose-6-phosphate Dehydrogenase and 6-Phosphogluconate Dehydrogenase from Methylobacillus flagellatum.
A.P. Sokolov and Y.A. Trotsenko, Glucose-6-phosphate Dehydrogenase and 6-Phosphogluconate Dehydrogenase from Arthrobacter globiformis.
D. Miethe and W. Babel, Glucose-6-phosphate Dehydrogenase from Pseudomonas W6.
G. M~aduller-Kraft and W. Babel, Citrate Synthases from Methylotrophs.
T. Leisinger and D. Kholer-Staub, Dichloromethane Dehalogenase from Hyphomicrobium DM2.
Assimilation of Formaldehyde in Methylotrophic Bacteria:
P.M. Goodwin, Assay of Assimilatory Enzymes in Crude Extracts of Serine Pathway Methylotrophs.
M.E. Lidstrom, Serine Hydroxymethyltransferases from Methylobacterium organophilum XX.
C. Krema and M.E. Lidstrom, Hydroxypyruvate Reductase from Methylobacterium extorquens AM1.
A.J. Hacking and J.R. Quayle, Malyl-A CoA Lyase from Methylobacterium extorquens AM1.
P.J. Arps, Synthesis of ~scL-4-MAlyl Coenzyme A.
N. Arfman, L. Bystrykh, N.I. Govoruhina, and L. Dijkhuizen, 3-Hexulose-6-phosphate Synthase from Thermotolerant Methylotroph Bacillus C1.
N. Kato, 3-Hexulose-6-phosphate Synthase from Mycobacterium gastri MB19.
R.H. M~aduller and W. Babel, 3-Hexulose-6-phosphate Synthase from Acetobacter methanolicus MB58.
P.R. Levering and L. Dijkhuizen, Transaldolase Isoenzymes from Arthrobacter PI.
Methylotrophic Enzymes in Methanol-Utilizing Yeast:
M. Veenhuis and I.J. van der Klei, Cytochemical Staining Methods for Localization of Key Enzymes of Methanol Metabolism in Hansenula polymorpha.
I.J. van der Klei, L.V. Bystrykh, and W. Harder, Alcohol Oxidase from Hansenula polymorpha CBS 4732.
P.J. Large and G.W. Haywood, Amine Oxidases from Methylotrophic Yeasts.
L.V. Bystrykh, W. De Koning, and W. Harder, Dihydroxacetone Synthase from Candida boidinii KD1.
L.V. Bystrykh, W. De Koning, and W. Harder, Triokinase from Candida boidinii KD1.
K.H. Hoffmann and W. Babel, Glycerone Kinase from Candida methylica.
N. Kato, Formaldehyde Dehydrogenase from Methylotrophic Yeasts.
N. Kato, Formate Dehydrogenase from Methylotrophic Yeasts.
M. Ueda, S. Mozaffar, and A. Tanaka, Catalase from Candida boidinii 2201. Each chapter includes references. Author Index. Subject Index.
This volume is the first comprehensive compilation of methods for the assay and purification of enzymes involved in the utilization of reduced one-carbon compounds and higher hydrocarbons. In the last decade there has been an explosion of interest in the organisms that grow on one-carbon compounds and in those that grow on higher hydrocarbons. This is due to the commercial interest in the unique enzymes involved in these specialty metabolic pathways and to a growing understanding of the important role these organisms play in carbon cycling in nature. More recent interest in the use of these organisms and their enzymes for detoxification of hazardous waste has once again put the spotlight on these unique microorganisms. This volume will prove to be a valuable source for researchers in academia, government, and industry alike.
Biochemists; basic research and industrial microbiologists (including those working at oil companies); environmental, organic, analytical, and microbial chemists.
- No. of pages:
- © Academic Press 1990
- 28th September 1990
- Academic Press
- Hardcover ISBN:
- eBook ISBN:
@from:Praise for the Volume @qu:"Recommeded for all individuals with an interest with eicosanoids and lipid mediators." @source:--AMERICAN JOURNAL OF PHYSIOLOGY @from:Praise for the Series @qu:"The Methods in Enzymology series represents the gold-standard." @source:--NEUROSCIENCE @qu:"Incomparably useful." @source:--ANALYTICAL BIOCHEMISTRY @qu:"It is a true 'methods' series, including almost every detail from basic theory to sources of equipment and reagents, with timely documentation provided on each page." @source:--BIO/TECHNOLOGY @qu:"The series has been following the growing, changing and creation of new areas of science. It should be on the shelves of all libraries in the world as a whole collection." @source:--CHEMISTRY IN INDUSTRY @qu:"The appearance of another volume in that excellent series, Methods in Enzymology, is always a cause for appreciation for those who wish to successfully carry out a particular technique or prepare an enzyme or metabolic intermediate without the tiresome prospect of searching through unfamiliar literature and perhaps selecting an unproven method which is not easily reproduced." @source:--AMERICAN SOCIETY OF MICROBIOLOGY NEWS @qu:"If we had some way to find the work most often consulted in the laboratory, it could well be the multi-volume series Methods in Enzymology...a great work." @source:--ENZYMOLOGIA @qu:"A series that has established itself as a definitive reference for biochemists." @source:--JOURNAL OF CHROMATOGRAPHY
California Institute of Technology, Division of Biology, Pasadena, U.S.A.
The Salk Institute, La Jolla, CA, USA
Keck Laboratories, California Institute of Technology, Pasadena, California, U.S.A.
Elsevier.com visitor survey
We are always looking for ways to improve customer experience on Elsevier.com.
We would like to ask you for a moment of your time to fill in a short questionnaire, at the end of your visit.
If you decide to participate, a new browser tab will open so you can complete the survey after you have completed your visit to this website.
Thanks in advance for your time.