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Lipases. Part A, Biotechnology /
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. 284. |
| Temas: | |
| Acceso en línea: | Texto completo Texto completo |
MARC
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| 245 | 0 | 0 | |a Lipases. |n Part A, |p Biotechnology / |c edited by Byron Rubin, Edward A. Dennis. |
| 260 | |a San Diego : |b Academic Press, |c �1997. | ||
| 300 | |a 1 online resource (xxxi, 408 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. 284 | |
| 504 | |a Includes bibliographical references and indexes. | ||
| 505 | 0 | |a Sect. 1. Primary and tertiary structure -- Structure as a basis for understanding interfacial properties of lipases -- Identification of conserved residues in family of esterase and lipase sequences -- Identification of important motifs in protein sequences: program MULTIM and its applications tolipase-related sequences -- Lipases and [alpha]/[beta] hydrolase fold -- Pancreatic lipases and their complexes with colipases and inhibitors: crystallization and crystal packing -- Impact of structural information on understanding lipolytic function -- Surface and electrostatics of cutinases -- Sect. 2. Isolation, cloning, expression, and engineering -- Site-specific mutagenesis of human pancreatic lipase -- Lipase eingineering: a window into structure-function relationships -- Purification of carboxyl ester lipase (bile salt-stimulated lipase) from human milk and pancreas -- Two novel lipases from thermophile Bacillus thermocatenulatus: screening, purification, cloning, overexpression, and properties -- Vernonia lipase: a plant lipase with strong fatty acid selectivity -- Hepatic lipase: high-level expression and subunit structure determination -- Cloning, sequencing, and expression of Candida rugosa lipases -- Influence of various signal peptides on secretion of mammalian acidic lipases in baculovirus-insect cell system -- Large-scale purification and kinetic properties of recombinant hormone-sensitive lipase from baculovirus-insect cell systems -- New pancreatic lipases: gene expression, protein secretion, and the newborn -- Structure and function of engineered Pseudomonas mendocina lipase -- Protein engineering of microbial lipases of industrial interest -- Glycosylation of bile salt-dependent lipase (cholesterol esterase) -- Steroselectivity of lipase from Rhizopus oryzae toward triaclglycerols and analogs: computer-aided modeling and experimental validation. | |
| 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 researchers in 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 | |
| 546 | |a English. | ||
| 650 | 0 | |a Lipase. | |
| 650 | 0 | |a Biotechnology. | |
| 650 | 0 | |a Lipase |x Biotechnology. | |
| 650 | 0 | |a Molecular cloning. | |
| 650 | 0 | |a Bioengineering. | |
| 650 | 1 | 2 | |a Lipase |x chemistry |0 (DNLM)D008049Q000737 |
| 650 | 2 | 2 | |a Cloning, Molecular |0 (DNLM)D003001 |
| 650 | 2 | |a Biotechnology |0 (DNLM)D001709 | |
| 650 | 6 | |a Lipase |0 (CaQQLa)201-0024705 |x Biotechnologie. |0 (CaQQLa)201-0378829 | |
| 650 | 6 | |a Lipase. |0 (CaQQLa)201-0024705 | |
| 650 | 6 | |a Biotechnologie. |0 (CaQQLa)201-0004007 | |
| 650 | 6 | |a Clonage mol�eculaire. |0 (CaQQLa)201-0032258 | |
| 650 | 7 | |a bioengineering. |2 aat |0 (CStmoGRI)aat300250623 | |
| 650 | 7 | |a Molecular cloning |2 fast |0 (OCoLC)fst01024762 | |
| 650 | 7 | |a Lipase |x Biotechnology |2 fast |0 (OCoLC)fst01751548 | |
| 650 | 7 | |a Bioengineering |2 fast |0 (OCoLC)fst00832028 | |
| 650 | 7 | |a Biotechnology |2 fast |0 (OCoLC)fst00832729 | |
| 650 | 7 | |a Lipase |2 fast |0 (OCoLC)fst00999359 | |
| 650 | 7 | |a Triacylglycerol lipase. |2 fmesh | |
| 650 | 7 | |a Clonage mol�eculaire. |2 fmesh | |
| 650 | 7 | |a Biotechnologie. |2 fmesh | |
| 650 | 7 | |a Lipases. |2 ram | |
| 650 | 7 | |a Biotechnologie. |2 ram | |
| 650 | 7 | |a Clonage mol�eculaire. |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 A, Biotechnology. |d San Diego : Academic Press, �1997 |z 0121821854 |w (OCoLC)37609759 |
| 830 | 0 | |a Methods in enzymology ; |v v. 284. | |
| 856 | 4 | 0 | |u https://sciencedirect.uam.elogim.com/science/book/9780121821852 |z Texto completo |
| 856 | 4 | 0 | |u https://sciencedirect.uam.elogim.com/science/bookseries/00766879/284 |z Texto completo |
| 856 | 4 | 0 | |u https://sciencedirect.uam.elogim.com/science/bookseries/00766879/284 |z Texto completo |
| 856 | 4 | 0 | |u https://sciencedirect.uam.elogim.com/science/book/9780121821852 |z Texto completo |