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Lipases. Part B, Enzyme characterization and utilization /
The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. More th...
| Clasificación: | Libro Electrónico |
|---|---|
| Otros Autores: | , |
| Formato: | Electrónico eBook |
| Idioma: | Inglés |
| Publicado: |
San Diego :
Academic Press,
�1997.
|
| Colección: | Methods in enzymology ;
v. 286. |
| Temas: | |
| Acceso en línea: | Texto completo Texto completo |
MARC
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| 245 | 0 | 0 | |a Lipases. |n Part B, |p Enzyme characterization and utilization / |c edited by Byron Rubin, Edward A. Dennis. |
| 260 | |a San Diego : |b Academic Press, |c �1997. | ||
| 300 | |a 1 online resource (xxxi, 563 pages) : |b illustrations. | ||
| 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 v. 286 | |
| 504 | |a Includes bibliographical references and indexes. | ||
| 505 | 0 | |a Sect. 1. Regulation and characterization -- Inhibition of lipid absorption as an approach to the treatment of obesity -- Regulation of hormone-sensitive lipase activity in adipose tissue -- Use of gene knockout mice to establish lipase function -- Properties of pancreatic carboxyl ester lipase in mRNA-injected Xenopus oocytes and transfected mammalian hepatic and intestinal cells -- Noncatalytic functions of lipoprotein lipase -- Radiation inactivation studies of hepatic cholesteryl ester hydrolases -- Immunological techniques for the characterization of digestive lipases -- Sect. 2. Substrate and inhibitor characterization -- Physical behavior of lipase substrates -- Phospholipase A₂ activity and physical properties of lipid-bilayer substances -- Covalent inactivation of lipases -- Mechanism-based inhibitors of mammalian cholesterol esterase -- On the inhibition of microbial lipases by tetrahydrolipstatin -- Monolayer techniques for studying lipase kinetics -- Recovery of monomolecular films in studies of lipolysis -- Oil-drop tensiometer: applications for studying the kinetics of lipase action -- A critical reevaluation of the phenomenon of interfacial activation -- Sect. 3. Biocatalytic utility -- Screening techniques for lipase catalyst selection -- Kinetics, molecular modeling, and synthetic applications with microbial lipases -- Ester synthesis via acyl transfer (transesterification) -- Cross-linked enzyme crystals of lipases as catalysts for kinetic resolution of acids and alcohols -- Measurement and control of hydration in non-aqueous biocatalysis -- Solvent effect in lipase-catalyzed racemate resolution -- Lipases in supercritical fluids -- Stabilization of lipases against deactivation of acetaldehyde formed in acyl transfer reactions. | |
| 588 | 0 | |a Print version record. | |
| 520 | |a The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. More than 270 volumes have been published (all of them still in print) and much of the material is relevant even today-truly an essential publication for researchersin all fields of life sciences. | ||
| 506 | |3 Use copy |f Restrictions unspecified |2 star |5 MiAaHDL | ||
| 533 | |a Electronic reproduction. |b [S.l.] : |c HathiTrust Digital Library, |d 2011. |5 MiAaHDL | ||
| 538 | |a Master and use copy. Digital master created according to Benchmark for Faithful Digital Reproductions of Monographs and Serials, Version 1. Digital Library Federation, December 2002. |u http://purl.oclc.org/DLF/benchrepro0212 |5 MiAaHDL | ||
| 583 | 1 | |a digitized |c 2011 |h HathiTrust Digital Library |l committed to preserve |2 pda |5 MiAaHDL | |
| 650 | 0 | |a Lipase. | |
| 650 | 0 | |a Enzymes. | |
| 650 | 2 | |a Lipase |x metabolism |0 (DNLM)D008049Q000378 | |
| 650 | 2 | |a Lipase |x pharmacokinetics |0 (DNLM)D008049Q000493 | |
| 650 | 2 | |a Lipase |x chemistry |0 (DNLM)D008049Q000737 | |
| 650 | 2 | |a Enzymes |0 (DNLM)D004798 | |
| 650 | 6 | |a Lipase. |0 (CaQQLa)201-0024705 | |
| 650 | 6 | |a Enzymes. |0 (CaQQLa)201-0002557 | |
| 650 | 7 | |a enzyme. |2 aat |0 (CStmoGRI)aat300212647 | |
| 650 | 7 | |a Enzymes. |2 fast |0 (OCoLC)fst00913605 | |
| 650 | 7 | |a Lipase. |2 fast |0 (OCoLC)fst00999359 | |
| 650 | 7 | |a Triacylglycerol lipase. |2 fmesh | |
| 650 | 7 | |a Enzymes. |2 fmesh | |
| 650 | 7 | |a Cin�etique enzymatique. |2 ram | |
| 650 | 7 | |a Lipides |x M�etabolisme. |2 ram | |
| 650 | 7 | |a Lipases. |2 ram | |
| 700 | 1 | |a Rubin, Byron. | |
| 700 | 1 | |a Dennis, Edward A. | |
| 773 | 0 | |t Methods in enzymology. | |
| 773 | 0 | |t Elsevier. | |
| 776 | 0 | 8 | |i Print version: |t Lipases. Part B, Enzyme characterization and utilization. |d San Diego : Academic Press, �1997 |z 0121821870 |w (OCoLC)37650066 |
| 830 | 0 | |a Methods in enzymology ; |v v. 286. | |
| 856 | 4 | 0 | |u https://sciencedirect.uam.elogim.com/science/book/9780121821876 |z Texto completo |
| 856 | 4 | 0 | |u https://sciencedirect.uam.elogim.com/science/bookseries/00766879/286 |z Texto completo |
| 856 | 4 | 0 | |u https://sciencedirect.uam.elogim.com/science/bookseries/00766879/286 |z Texto completo |
| 856 | 4 | 0 | |u https://sciencedirect.uam.elogim.com/science/book/9780121821876 |z Texto completo |