Proteolytic enzymes. Serine and cysteine peptidases / Volume 244 :
The critically acclaimed laboratory standard, 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. The series contains much materia...
Clasificación: | Libro Electrónico |
---|---|
Otros Autores: | |
Formato: | Electrónico eBook |
Idioma: | Inglés |
Publicado: |
San Diego :
Academic Press,
�1994.
|
Colección: | Methods in enzymology ;
v. 244. |
Temas: | |
Acceso en línea: | Texto completo Texto completo |
MARC
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020 | |a 9780121821456 |q (electronic bk.) | ||
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060 | 4 | |a W1 ME9615K v.244 1994 | |
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084 | |a 35.74 |2 bcl | ||
245 | 0 | 0 | |a Proteolytic enzymes. |n Volume 244 : |b Serine and cysteine peptidases / |c edited by Alan J. Barrett. |
246 | 3 | 0 | |a Serine and cysteine peptidases |
260 | |a San Diego : |b Academic Press, |c �1994. | ||
300 | |a 1 online resource (xxxi, 765 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, |x 0076-6879 ; |v v. 244 | |
504 | |a Includes bibliographical references and index. | ||
520 | |a The critically acclaimed laboratory standard, 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. The series contains much material still relevant today--truly an essential publication for researchers in all fields of life sciences. Key Features * Presents new ideas on classification of proteolytic enzymes * Covers 100 individual proteolytic enzymes * Offers numerous medical implications of work in this area * Provides uses of these enzymes in biotechnology. | ||
588 | 0 | |a Print version record. | |
505 | 0 | |a 1. Classification of Peptidases / Alan J. Barrett -- 2. Families of Serine Peptidases / Alan J. Barrett / Neil D. Rawlings -- 3. Myeloblastin: Leukocyte Proteinase 3 / Beulah Gray / John R. Hoidal / N.V. Rao -- 4. Granzyme A / Markus M. Simon / Michael D. Kramer -- 5. Granzyme B / Juerg Tschopp / Manuel C. Peitsch -- 6. Tryptase: A Mast Cell Serine Protease / Lawrence B. Schwartz -- 7. Hepsin / Adrian Torres-Rosado / Akihiko Tsuji / Kotoku Kurachi -- 8. Glutamyl Endopeptidases / Klaus Breddam / Jens J. Birktoft -- 9. Lysyl Endopeptidase of Achromobacter lyticus / Fumio Sakiyama / Takeharu Masaki -- 10. IgA-Specific Prolyl Endopeptidases: Serine Type / Andrew G. Plaut / William W. Bachovchin -- 11. Biochemical and Genetic Methods for Analyzing Specificity and Activity of Precursor-Processing Enzyme: Yeast Kex2 Protease, Kexin / Alison Bevan / Charles Brenner / Robert S. Fuller -- 12. Purification of Recombinant Soluble, Forms of Furin Produced in Chinese Hamster Ovary Cells / Kazuhisa Nakayama -- 13. Pro-Protein Convertases of Subtilisin/Kexin Family / Michel Chretien / Nabil G. Seidah -- 14. Prolyl Oligopeptidases / Laszlo Polgar -- 15. Oligopeptidase B: Protease II from Escherichia coli / Daisuke Tsuru / Tadashi Yoshimoto -- 16. Dipeptidyl-peptidase IV from Rat Liver / Yoshio Misumi / Shigenori Ogata / Yukio Ikehara -- 17. Acylaminoacyl-peptidase / Wanda M. Jones / Andrea Scaloni / James M. Manning -- 18. Carboxypeptidases C and D / S. James Remington / Klaus Breddam -- 19. Serine-Type D-Ala-D-Ala Peptidases and Penicillin-Binding Proteins / Benoit Granier / Marc Jamin / Maggy Adam / Moreno Galleni / Bernard Lakaye / Willy Zorzi / Jacqueline Grandchamps / Jean-Marc Wilkin / Claudine Fraipont / Bernard Joris / Colette Duez / Martine Nguyen-Disteche / Jacques Coyette / Melina Leyh-Bouille / Jean Dusart / Leon Christiaens / Jean-Marie Frere / Jean-Marie Ghuysen -- 20. Cleavage of LexA Repressor / John W. Little / Baek Kim / Kenneth L. Roland / Margaret H. Smith / Lih-Ling Lin / Steve N. Slilaty -- 21. Bacterial Leader Peptidase I / William R. Tschantz / Ross E. Dalbey -- 22. Eukaryote Microsomal Signal Peptidases / Mark O. Lively / Ann L. Newsome / Mohamad Nusier -- 23. Endopeptidase Clp: ATP-Dependent Clp Protease from Escherichia coli / Michael R. Maurizi / Mark W. Thompson / Satyendra K. Singh / Seung-Ho Kim -- 24. Multicatalytic Endopeptidase Complex: Proteasome / A. Jennifer Rivett / Peter J. Savory / Hakim Djaballah -- 25. ATP-Dependent Protease La (Lon) from Escherichia coli / Alfred L. Goldberg / Richard P. Moerschell / Chin Ha Chung / Michael R. Maurizi -- 26. Mitochondrial ATP-Dependent Protease from Rat Liver and Yeast / Stefan Kuzela / Alfred L. Goldberg -- 27. Omptin: An Escherichia coli Outer Membrane Proteinase That Activates Plasminogen / Walter F. Mangel / Diana L. Toledo / Mark T. Brown / Kimberly Worzalla / Mijin Lee / John J. Dunn -- 28. Transient Transfection Assay of the Herpesvirus Maturational Proteinase, Assemblin / Wade Gibson / Anthony R. Welch / Jennifer Ludford -- 29. Purification and Kinetic Characterization of Human Cytomegalovirus Assemblin / Michele C. Smith / Joanna Giordano / James A. Cook / Mark Wakulchik / Elcira C. Villarreal / Gerald W. Becker / Kerry Bemis / Jean Labus / Joseph S. Manetta -- 30. Amino Acid and Peptide Phosphonate Derivatives as Specific Inhibitors of Serine Peptidases / Jozef Oleksyszyn / James C. Powers -- 31. Isocoumarin Inhibitors of Serine Peptidases / James C. Powers / Chih-Min Kam -- 32. Families of Cysteine Peptidases / Neil D. Rawlings / Alan J. Barrett -- 33. Catalytic Mechanism in Papain Family of Cysteine Peptidases / Andrew C. Storer / Robert Menard -- 34. Cathepsin S and Related Lysosomal Endopeptidases / Heidrun Kirschke / Bernd Wiederanders -- 35. Cysteine Endopeptidases of Entamoeba histolytica / Henning Scholze / Egbert Tannich -- 36. Cysteine Endopeptidases of Parasitic Protozoa / Michael J. North -- 37. Glycyl Endopeptidase / David J. Buttle -- 38. Pineapple Cysteine Endopeptidases / Andrew D. Rowan / David J. Buttle -- 39. Cancer Procoagulant / Stuart G. Gordon -- 40. Picornains 2A and 3C / Tim Skern / Hans-Dieter Liebig -- 41. Adenovirus Endopeptidases / Joseph M. Weber / Karoly Tihanyi -- 42. Legumain: Asparaginyl Endopeptidase / Shin-Ichi Ishii -- 43. Interleukin-1[beta] Converting Enzyme / Nancy A. Thornberry -- 44. Isoprenylated Protein Endopeptidase / Robert R. Rando / Yu-Ting Ma -- 45. Affinity Chromatography of Cysteine Peptidases / David J. Buttle -- 46. Peptidyl Diazomethanes as Inhibitors of Cysteine and Serine Proteinases / Elliott Shaw -- 47. Peptidyl (Acyloxy)methanes as Quiescent Affinity Labels for Cysteine Proteinases / Allen Krantz -- 48.N, O-Diacyl Hydroxamates as Selective and Irreversible Inhibitors of Cysteine Proteinases / Dieter Bromme / Hans-Ulrich Demuth -- 49. Cystatins / Magnus Abrahamson. | |
650 | 0 | |a Peptidase. | |
650 | 0 | |a Proteolytic enzymes. | |
650 | 0 | |a Serine proteinases. | |
650 | 0 | |a Cysteine proteinases. | |
650 | 0 | |a Peptidase |x Classification. | |
650 | 1 | 2 | |a Serine Endopeptidases |0 (DNLM)D012697 |
650 | 1 | 2 | |a Cysteine Endopeptidases |0 (DNLM)D003546 |
650 | 2 | 2 | |a Peptide Hydrolases |0 (DNLM)D010447 |
650 | 6 | |a Peptidases �a s�erine. |0 (CaQQLa)201-0035837 | |
650 | 6 | |a Peptidases �a cyst�eine. |0 (CaQQLa)201-0262738 | |
650 | 6 | |a Peptidases |0 (CaQQLa)201-0032233 |x Classification. |0 (CaQQLa)201-0378392 | |
650 | 6 | |a Peptidases. |0 (CaQQLa)201-0032233 | |
650 | 6 | |a Enzymes prot�eolytiques. |0 (CaQQLa)201-0055592 | |
650 | 7 | |a Serine proteinases. |2 fast |0 (OCoLC)fst01113206 | |
650 | 7 | |a Cysteine proteinases. |2 fast |0 (OCoLC)fst00886184 | |
650 | 7 | |a Peptidase. |2 fast |0 (OCoLC)fst01057550 | |
650 | 7 | |a Proteolytic enzymes. |2 fast |0 (OCoLC)fst01079783 | |
650 | 7 | |a Peptide hydrolases. |2 fmesh | |
650 | 7 | |a Serine endopeptidases. |2 fmesh | |
650 | 7 | |a Cysteine endopeptidases. |2 fmesh | |
650 | 7 | |a Enzymes. |2 fmesh | |
650 | 7 | |a Proteasen |2 gnd |0 (DE-588)4047521-9 | |
650 | 7 | |a Serinproteinasen |2 gnd |0 (DE-588)4181042-9 | |
650 | 7 | |a Cysteinproteasen |2 gnd |0 (DE-588)4130449-4 | |
650 | 1 | 7 | |a Proteolyse. |2 gtt |
650 | 1 | 7 | |a Peptidasen. |2 gtt |
650 | 1 | 7 | |a Cysteine. |2 gtt |
650 | 1 | 7 | |a Serine. |2 gtt |
650 | 7 | |a Enzymologia |v podr�eczniki laboratoryjne. |2 jhpk | |
650 | 7 | |a Peptydazy. |2 jhpk | |
650 | 7 | |a Peptidases. |2 ram | |
650 | 7 | |a Cyst�eine endopeptidases. |2 ram | |
650 | 7 | |a S�erine endopeptidases. |2 ram | |
650 | 7 | |a Enzymes. |2 ram | |
650 | 0 | 7 | |a Proteasen. |2 swd |
650 | 0 | 7 | |a Serinproteinasen. |2 swd |
650 | 0 | 7 | |a Cysteinproteasen. |2 swd |
653 | 0 | |a Enzymes | |
653 | 0 | 0 | |a proteinases |
653 | 0 | 0 | |a pepsine |
653 | 0 | 0 | |a pepsin |
653 | 0 | 0 | |a papain |
653 | 0 | 0 | |a trypsine |
653 | 0 | 0 | |a trypsin |
653 | 0 | 0 | |a cystine |
653 | 0 | 0 | |a cysteine |
653 | 0 | 0 | |a methionine |
653 | 0 | 0 | |a enzymactiviteit |
653 | 0 | 0 | |a enzyme activity |
653 | 1 | 0 | |a Proteins and Enzymes |
653 | 1 | 0 | |a Eiwitten en enzymen |
655 | 7 | |a Classification. |2 fast |0 (OCoLC)fst01697073 | |
700 | 1 | |a Barrett, Alan J., |e editor. | |
776 | 0 | 8 | |i Print version: |t Proteolytic enzymes. |d San Diego : Academic Press, �1994 |z 0121821455 |w (OCoLC)31473281 |
830 | 0 | |a Methods in enzymology ; |v v. 244. |x 0076-6879 | |
856 | 4 | 0 | |u https://sciencedirect.uam.elogim.com/science/book/9780121821456 |z Texto completo |
856 | 4 | 0 | |u https://sciencedirect.uam.elogim.com/science/bookseries/00766879/244 |z Texto completo |