MARC record from Internet Archive

LEADER: 12265cam 2201249 a 4500
001 ocm24591346
003 OCoLC
005 20181218233626.0
008 911003s1990 caua b 001 0 eng
007 cr cn ||||||||
010 $a 54009110
040 $aNLM$beng$cNLM$dMCS$dAGL$dVET$dUKM$dNLGGC$dBAKER$dLVB$dCGC$dYDXCP$dCS1$dCUY$dGEBAY$dBDX$dGBVCP$dOCLCF$dBEDGE$dDEBBG$dOCLCQ$dOCLCO$dOCLCQ$dCAI$dOCLCQ$dCASUM$dOCLCO$dOCLCA$dNLM$dCPO$dQE2$dUKMGB
015 $aGB9166959$2bnb
016 7 $a9112913$2DNLM
016 7 $a012-18208$2Uk
016 7 $a006180488$2Uk
019 $a22469016$a22517218$a26317127$a953564992
020 $a9780121820893$q(alk. paper)
020 $a0121820890$q(alk. paper)
035 $a(OCoLC)24591346$z(OCoLC)22469016$z(OCoLC)22517218$z(OCoLC)26317127$z(OCoLC)953564992
050 4 $aQP601$b.C733 v.188
060 00 $aW1$bME9615K v.188 1990
060 10 $aQU 135$bH995 1990
070 0 $aQP601.M49$bv.188
072 0 $aX300
082 04 $a576.162$220
084 $aCHE 610f$2stub
084 $aCHE 660f$2stub
084 $aCHE 815f$2stub
084 $aCHE 825f$2stub
084 $aVK 8700$2rvk
084 $aWC 4355$2rvk
084 $aWD 5050$2rvk
245 00 $aHydrocarbons and methylotrophy /$cedited by Mary E. Lidstrom.
260 $aSan Diego :$bAcademic Press,$c℗♭1990.
300 $axxxii, 504 pages :$billustrations.
336 $atext$btxt$2rdacontent
337 $aunmediated$bn$2rdamedia
338 $avolume$bnc$2rdacarrier
490 1 $aMethods in enzymology ;$vv. 188
504 $aIncludes bibliographical references and indexes.
505 00 $tHydrocarbon monooxygenase system of Pseudomonas oleovorans /$rSheldon W. May, Andreas G. Katopodis and Mary E. Lidstrom --$tAssay methods for long-chain alkane oxidation in Acinetobacter /$rW.R. Finnerty and Mary E. Lidstrom --$tPrimary alcohol dehydrogenases from Acinetobacter /$rW.R. Finnerty and Mary E. Lidstrom --$tAldehyde dehydrogenases from Acinetobacter /$rW.R. Finnerty and Mary E. Lidstrom --$tPropane-specific alcohol dehydrogenase from Rhodococcus rhodochrous PNKb 1 /$rW. Ashraf, J.C. Murrell and Mary E. Lidstrom --$tCell-free assay methods for enzymes of propane utilization /$rJ.C. Murrell, W. Ashraf and Mary E. Lidstrom --$tQuinoprotein alcohol dehydrogenase from Pseudomonas aeruginosa and quinohemoprotein alcohol dehydrogenase from Pseudomonas testosteroni /$rB.W. Groen, Duine J.A. and Mary E. Lidstrom --$tToluene dioxygenase from Pseudomonas putida F1 /$rLawrence P. Wackett and Mary E. Lidstrom --$tNaphthalene dioxygenase from Pseudomonas NCIB 9816 /$rBurt D. Ensley, Billy E. Haigler and Mary E. Lidstrom --$tBenzene dioxygenase from Pseudomonas putida ML2 (NCIB 12190) /$rPhilip J. Geary [and others] --$tPhthalate dioxygenase /$rChristopher J. Batie, David P. Ballou and Mary E. Lidstrom --$tCyclohexanone 1,2-monooxygenase from Acinetobacter NCIMB 9871 /$rPeter W. Trudgill and Mary E. Lidstrom --$tCyclopentanone 1,2-monooxygenase from Pseudomonas NCIMB 9872 /$rPeter W. Trudgill and Mary E. Lidstrom --$tProtocatechuate 3,4-dioxygenase from Brevibacterium fuscum /$rJames W. Whittaker [and others] --$tProtocatechuate 4,5-dioxygenase from Pseudomonas testosterone /$rDavid M. Arciero [and others] --$tProtocatechuate 2,3-dioxygenase from Bacillus macerans /$rSanford A. Wolgel, John D. Lipscomb and Mary E. Lidstrom --$tGentisate 1,2-dioxygenase from Pseudomonas acidovorans /$rMark R. Harpel, Lipscomb John D. and Mary E. Lidstrom --$tSynthesis of 17O- or 18O-Enriched dihydroxy aromatic compounds /$rAllen M. Orville [and others] --$tCatechol 2,3-dioxygenases from Pseudomonas aeruginosa 2x /$rI.A. Kataeva, Golovleva L.A. and Mary E. Lidstrom --$tCatechol and chlorocatechol 1,2-Dioxygenases /$rKa-Leung Ngai [and others] --$tMuconate cycloisemerase /$rRichard B. Meagher [and others].
505 00 $tMuconolactone Isomerase /$rRichard B. Meagher [and others] --$tcis-1,2-Dihydroxycyclohexa-3,5-diene (NAD) oxidoreductase (cis-benzene dihydrodiol dehydrogenase) from Pseudomonas putida NCIB 12190 /$rJeremy R. Mason, Geary Philip J. and Mary E. Lidstrom --$tHydroxybenzoate hydroxylase /$rBarrie Entsch and Mary E. Lidstrom --$tPolycyclic aromatic hydrocarbon degradation by Mycobacterium /$rCarl Ecerniglia, Heitkamp Michael A. and Mary E. Lidstrom --$tBenzoate-CoA ligase from Rhodopseudomonas palustris /$rJane Gibson [and others] --$tLignin peroxidase from fungi: Phanerochaete chrysosporium /$rT. Kent Kirk [and others] --$tLong-chain alcohol dehydrogenase of Candida yeast /$rMitsuyoshi Ueda, Atsuo Tanaka and Mary E. Lidstrom --$tLong-chain aldehyde dehydrogenase of candida yeast /$rMitsuyoshi Ueda, Atsuo Tanaka and Mary E. Lidstrom --$tSoluble methane monooxygenase from Methylococcus capsulatus bath /$rSimon J. Pilkington, Howard Dalton and Mary E. Lidstrom --$tMethane monooxygenase from Methylosinus trichosporium OB3b /$rBrian G. Fox [and others] --$tMethanol dehydrogenase from Hyphomicrobium X /$rJ. Frank, Duine J.A. and Mary E. Lidstrom --$tMethanol dehydrogenase from Methylobacterium extorquens AM1 /$rDarren J. Day, Christopher Anthony and Mary E. Lidstrom --$tModifier protein for methanol dehydrogenase of methylotrophs /$rAntony R. Long, Christopher Anthony and Mary E. Lidstrom.
505 00 $tMethanol dehydrogenase from thermotolerant METHYLOTROPH Bacillus C1 /$rN. Arfman, L. Dijkhuizen and Mary E. Lidstrom --$tMethylamine oxidase from Arthrobacter P1 /$rWilliam S. McIntire and Mary E. Lidstrom --$tMethylamine dehydrogenase from Thiobacillus versutus /$rJohn E. van Wielink [and others] --$tMethylamine dehydrogenases from methylotrophic bacteria /$rVictor L. Davidson and Mary E. Lidstrom --$tMethylamine dehydrogenase from methylobacillus flagellatum /$rMichael Y. Kiriukhin [and others] --$tTrimethylamine dehydrogenase from bacterium W3A1 /$rWilliam S. McIntire and Mary E. Lidstrom --$tIsolation, preparation, and assay of pyrroloquinoline quinone /$rR.A. Van Der Meer [and others] --$tBlue copper proteins involved in methanol and methylamine oxidation /$rChristopher Anthony and Mary E. Lidstrom --$tSoluble Cytochromes c from methylomonas A4 /$rAlan A. Dispirito and Mary E. Lidstrom --$tSoluble cytochromes c of methanol-utilizing bacteria /$rDarren J. Day, Christopher Anthony and Mary E. Lidstrom --$tCytochrome cL and cytochrome cH from Hyphomicrobium X /$rJ. Frank, Duine J.A. and Mary E. Lidstrom --$tElectron-transfer flavoproteins from methylophilus methylotrophus and bacterium W3A1 /$rMazhar Husain and Mary E. Lidstrom --$tFormaldehyde dehydrogenases from methylotrophs /$rMargaret M. Attwood and Mary E. Lidstrom --$tNAD-linked, factor-independent, and glutathione-independent aldehyde dehydrogenase from Hyphomicrobium X /$rJ.A. Duine and Mary E. Lidstrom --$tFormate dehydrogenase from Methylosinus trichosporium OB3b /$rDavid R. Jollie, John D. Lipscomb and Mary E. Lidstrom --$tGlucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase from Methylobacillus flagellatum /$rLudmila V. Kletsova [and others] --$tGlucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase from Arthrobacter globiformis /$rA.P. Sokolov, Y.A. Trotsenko and Mary E. Lidstrom --$tGlucose-6-phosphate dehydrogenase from Pseudomonas W6 /$rDietmar Miethe, Babel Wolfgang and Mary E. Lidstrom --$tCitrate synthases from methylotrophs /$rGabriele Mu ller-Kraft, Wolfgang Babel and Mary E. Lidstrom.
505 00 $tDichloromethane dehalogenase from Hyphomicrobium DM2 /$rThomas Leisinger, Kohler-Staub Doris and Mary E. Lidstrom --$tAssay of assimilatory enzymes in crude extracts of serine pathway methylotrophs /$rPatricia M. Goodwin and Mary E. Lidstrom --$tSerine hydroxymethyltransferases from Methylobacterium organophilum XX /$rMary E. Lidstrom and Mary E. Lidstrom --$tHydroxypyruvate reductase from Methylobacterium extorquens AM 1 /$rCinder Krema and Mary E. Lidstrom --$tMalyl-CoA lyase from methylobacterium extorquens AM 1 /$rA.J. Hacking, J.R. Quayle and Mary E. Lidstrom --$tSynthesis of -4-Malyl coenzyme A /$rPeggy J. Arps and Mary E. Lidstrom --$t3-Hexulose-6-phosphate synthase from thermotolerant methylotroph Bacillus C1 /$rN. Arfman [and others] --$t3-Hexulose-6-phosphate synthase from mycobacterium gastri MB 19 /$rNobuo Kato and Mary E. Lidstrom --$t3-Hexulose-6-phosphate synthase from Acetobacter methanolicus MB58 /$rRoland H. Mu ller, Wolfgang Babel and Mary E. Lidstrom --$tTransaldolase Isoenzymes from Arthrobacter P1 /$rP.R. Levering, L. Dijkhuizen and Mary E. Lidstrom --$tCytochemical staining methods for localization of key enzymes of methanol metabolism in hansenula polymorpha /$rMarten Veenhuis, Ida J. Van Der Klei and Mary E. Lidstrom --$tAlcohol Oxidase from Hansenula polymorpha MIE 4732 /$rIda J. van der Klei [and others] --$tAmine oxidases from methylotrophic yeasts /$rPeter J. Large, Geoffrey Whaywood and Mary E. Lidstrom --$tDihydroxyacetone synthase from Candida boidinii KD1 /$rLeonid V. Bystrykh [and others] --$tTriokinase from Candida boidinii KD1 /$rLeonid V. Bystrykh [and others] --$tGlycerone kinase from Candida methylica /$rKlaus H. Hofmann, Wolfgang Babel and Mary E. Lidstrom --$tFormaldehyde dehydrogenase from methylotrophic yeasts /$rNobuo Kato and Mary E. Lidstrom --$tFormate dehydrogenase from methylotrophic yeasts /$rNobuo Kato and Mary E. Lidstrom --$tCatalase from Candida boidinii 2201 /$rMitsuyoshi Ueda [and others].
650 0 $aHydrocarbons$xBiodegradation.
650 0 $aMethylotrophic bacteria.
650 6 $aMe thane.
650 6 $aMe thylamines.
650 6 $aHydrocarbures.
650 7 $aEnzymes.$2eclas
650 7 $aBiochimie.$2eclas
650 7 $aHydrocarbons$xBiodegradation.$2fast$0(OCoLC)fst00964830
650 7 $aMethylotrophic bacteria.$2fast$0(OCoLC)fst01018781
650 17 $aMethylotrofe bacterie n.$2gtt
650 17 $aStofwisseling.$2gtt
650 17 $aEnzymen.$2gtt
650 17 $aBepaling.$2gtt
650 17 $aZuiveringstechnieken.$2gtt
650 7 $aEnzym$2gnd
650 7 $aHefeartige Pilze$2gnd
650 7 $aKohlenwasserstoffe$2gnd
650 7 $aMethanol$2gnd
650 7 $aMethylierung$2gnd
650 7 $aMethylotrophe Bakterien$2gnd
650 7 $aMethylotrophie$2gnd
650 7 $aMikroorganismus$2gnd
650 7 $aVerwertung$2gnd
650 7 $aAufsatzsammlung$2gnd
650 2 $aEnzymes.$0https://id.nlm.nih.gov/mesh/D004798
650 2 $aEuryarchaeota$xmetabolism.$0https://id.nlm.nih.gov/mesh/D019605Q000378
650 2 $aHydrocarbons$xmetabolism.$0https://id.nlm.nih.gov/mesh/D006838Q000378
650 07 $aKohlenwasserstoffe.$2swd
650 07 $aEnzym.$2swd
650 07 $aAufsatzsammlung.$2swd
650 07 $aMethylotrophie.$2swd
650 07 $aMikroorganismus.$2swd
650 07 $aVerwertung.$2swd
650 07 $aHefeartige Pilze.$2swd
650 07 $aMethanol.$2swd
650 07 $aMethylotrophe Bakterien.$2swd
650 07 $aMethylierung.$2swd
653 0 $aBiotechnology$aUse of$aEnzymes
655 4 $aAufsatzsammlung.
700 1 $aLidstrom, Mary E.
830 0 $aMethods in enzymology ;$vv. 188.
856 41 $3Table of contents$uhttp://www.gbv.de/dms/bowker/toc/9780121820893.pdf
856 41 $uhttp://www.sciencedirect.com/science/publication?issn=00766879&volume=188
856 41 $uhttps://www.sciencedirect.com/science/publication?issn=00766879&volume=188$zAccess restricted to Stanford community$yFulltext
856 4 $uhttps://www.sciencedirect.com/science/bookseries/00766879/188
856 41 $zSearch for this title in:$uhttp://qe2a-proxy.mun.ca/Login?url=http://www.sciencedirect.com/science/journal/00766879
856 $31850-9999$uhttp://www.elsevier.com/journals$xBLDSS
938 $aBaker & Taylor$bBKTY$c153.00$d153.00$i0121820890$n0001810693$sactive
938 $aBrodart$bBROD$n42299616$c$153.00
938 $aYBP Library Services$bYANK$n55433
029 0 $aNLM$b9112913
029 1 $aAU@$b000008021148
029 1 $aAU@$b000054284781
029 1 $aDEBBG$bBV004140249
029 1 $aGBVCP$b026117819
029 1 $aGEBAY$b1455189
029 1 $aHEBIS$b014101033
029 1 $aNLGGC$b078325188
029 1 $aNZ1$b3927074
029 1 $aUKMGB$b006180488
994 $aZ0$bP4A
948 $hNO HOLDINGS IN P4A - 376 OTHER HOLDINGS