Proteolytic enzymes : Aspartic and metallo peptidases /
In this volume of Methods in Enzymology and its companion Volume 244, the chapters on specific methods, enzymes, and inhibitors are organized within the rational framework of the new systems for classification and nomenclature. A wide variety of specificities of peptide bond hydrolysis are represent...
Clasificación: | Libro Electrónico |
---|---|
Otros Autores: | |
Formato: | Electrónico eBook |
Idioma: | Inglés |
Publicado: |
San Diego :
Academic Press,
�1995.
|
Colección: | Methods in enzymology ;
v. 248. |
Temas: | |
Acceso en línea: | Texto completo Texto completo |
MARC
LEADER | 00000cam a2200000 a 4500 | ||
---|---|---|---|
001 | SCIDIR_ocn776047245 | ||
003 | OCoLC | ||
005 | 20231117044706.0 | ||
006 | m o d | ||
007 | cr un||||a|a|| | ||
008 | 120212s1995 caua ob 001 0 eng d | ||
040 | |a OCLCE |b eng |e pn |c OCLCE |d CUSER |d AZU |d OPELS |d OCLCQ |d OPELS |d OCLCF |d OCLCQ |d OCLCO |d KUK |d OCLCQ |d OCLCO |d OCLCA |d BUF |d OCLCO |d OCLCQ |d ANS |d OCLCA |d DCT |d OCLCQ |d UHL |d UKBTH |d CUV |d EUN |d OCLCQ |d OCLCO |d SFB |d OCLCQ |d IND |d OCLCO | ||
066 | |c (S | ||
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020 | |a 0121821498 |q (electronic bk.) | ||
020 | |a 9780121821494 |q (electronic bk.) | ||
035 | |a (OCoLC)776047245 |z (OCoLC)56565414 |z (OCoLC)326630789 |z (OCoLC)988571477 |z (OCoLC)1021279184 |z (OCoLC)1113263522 |z (OCoLC)1113622727 |z (OCoLC)1125499286 | ||
042 | |a dlr | ||
050 | 4 | |a QP601 |b .C733 vol. 248 | |
060 | 4 | |a W1 |b ME9615K v.248 1995 | |
060 | 4 | |a QU 136 |b P96783 1995 | |
070 | |a QP601.M49 |b v.248 | ||
072 | 0 | |a X300 | |
082 | 0 | 4 | |a 574.19256 |2 20 |
084 | |a 35.74 |2 bcl | ||
084 | |a WC 4355 |2 rvk | ||
084 | |a WD 5050 |2 rvk | ||
245 | 0 | 0 | |a Proteolytic enzymes : |b Aspartic and metallo peptidases / |c edited by Alan J. Barrett. |
246 | 3 | 0 | |a Aspartic and metallo peptidases |
260 | |a San Diego : |b Academic Press, |c �1995. | ||
300 | |a 1 online resource (xxxi, 873 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. 248 | |
504 | |a Includes bibliographical references and indexes. | ||
520 | |a In this volume of Methods in Enzymology and its companion Volume 244, the chapters on specific methods, enzymes, and inhibitors are organized within the rational framework of the new systems for classification and nomenclature. A wide variety of specificities of peptide bond hydrolysis are represented in each set of peptidases, together with an equally wide range of biological functions. Key Features * Aspartic peptidases * Metallopeptidases * New information on classification of proteolytic enzymes * Medical implications of research in this area * Biotechnological uses of these enzymes. | ||
588 | 0 | |a Print version record. | |
506 | |3 Use copy |f Restrictions unspecified |2 star |5 MiAaHDL | ||
533 | |a Electronic reproduction. |b [Place of publication not identified] : |c HathiTrust Digital Library, |d 2012. |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 2012 |h HathiTrust Digital Library |l committed to preserve |2 pda |5 MiAaHDL | |
546 | |a English. | ||
505 | 0 | |a Peptide thioester substrates for serine peptidases and metalloendopeptidases / James C. Powers, Chih-Min Kam -- Fluorimetric assays of proteolytic enzymes / C. Graham Knight -- Defined substrate mixtures for mapping of proteinase specificities / Gerard M. McGeehan, D. Mark Bickett, Jeffrey S. Wiseman, Michael Green, Judd Berman -- Assay of proteoglycan degradation / Christopher J. Handley, David J. Buttle -- Theoretical and practical aspects of proteinase inhibition kinetics / Joseph G. Bieth -- Active-site titration of peptidases / C. Graham Knight -- Families of aspartic peptidases, and those of unknown catalytic mechanism / Neil D. Rawlings, Alan J. Barrett -- Procathepsin E and cathepsin E / Takashi Kageyama -- Processing enzymes of pepsin family: Yeast aspartic protease 3 and pro-opiomelanocortin converting enzyme / Y. Peng Loh, Niamh X. Cawley -- Proteinase A from Aspergillus niger / Kenji Takahashi -- Thermopsin / Xinli Lin, Jordan Tang -- Bacterial prolipoprotein signal peptidase / Krishnan Sankaran, Henry C. Wu -- Evolutionary families of metallopeptidases / Neil D. Rawlings, Alan J. Barrett -- Removal and replacement of metal ions in metallopeptidases / David S. Auld -- Pseudolysin and other pathogen endopeptidases of thermolysin family / Kazuyuki Morihara -- Neprilysin: Assay methods, purification, and characterization / Chingwen Li, Louis B. Hersh -- Inhibitors of neprilysin: Design, pharmacological and clinical applications / Bernard P. Roques, Florence Noble, Philippe Crine, Marie-Claude Fourni�e-Zaluski -- Peptidyl dipeptidase A: Angiotensin I-converting enzyme / Pierre Corvol, Tracy A. Williams, Florent Soubrier -- Astacin / Walter St�ocker, Robert Zwilling -- Meprins A and B / Russell L. Wolz, Judith S. Bond -- Snake venom metalloendopeptidases: Reprolysins / J�on B. Bjarnason, Jay W. Fox -- Atrolysins: Metalloproteinases from Crotalus atrox venom / Jay W. Fox, J�on B. Bjarnason -- Membrane-associated metalloproteinase recognized by characteristic cleavage of myelin basic protein: Assay and isolation / Linda Howard, Paul Glynn -- Serralysin and related bacterial proteinases / Hiroshi Maeda, Kazuyuki Morihara -- Vertebrate collagenases / Marianna Dioszegi, Paul Cannon, Harold E. Van Wart -- Human neutrophil collagenase / Harald Tschesche -- Human stromelysins 1 and 2 / Hideaki Nagase -- Gelatinases A and B / Gillian Murphy, Thomas Crabbe -- Matrilysin / J. Frederick Woessner Jr. -- Tissue inhibitors of matrix metalloendopeptidases / Gillian Murphy, Frances Willenbrock -- Quantification of matrix metalloproteinases in tissue samples / J. Frederick Woessner Jr. -- Thimet oligopeptidase and oligopeptidase M or neurolysin / Alan J. Barrett, Molly A. Brown, Pamela M. Dando, C. Graham Knight, Norman McKie, Neil D. Rawlings, Atsushi Serizawa -- Mitochondrial intermediate peptidase / Grazia Isaya, Frantisek Kalousek -- Dipeptidyl carboxypeptidase and oligopeptidase A from Escherichia coli and Salmonella typhimurium / Christopher A. Conlin, Charles G. Miller -- Oligopeptidases from Lactococcus lactis / V�eronique Monnet -- Neurolysin: Purification and assays / F. Checler, H. Barelli, P. Dauch, V. Dive, B. Vincent, J.P. Vincent -- Leishmanolysin: Surface metalloproteinase of Leishmania / Jacques Bouvier, Pascal Schneider, Robert Etges -- Immunoglobulin A-metallo-type specific prolyl endopeptidases / Andrew G. Plaut, Andrew Wright -- Tetanus and botulism neurotoxins: Isolation and assay / Giampietro Schiavo, Cesare Montecucco -- Human carboxypeptidase N: Lysine carboxypeptidase / Randal A. Skidgel -- Human carboxypeptidase M / Fulong Tan, Peter A. Deddish, Randal A. Skidgel -- Carboxypeptidase T / Valentin M. Stepanov -- Pitrilysin / Angela Anastasi, Alan J. Barrett -- Insulysin and pitrilysin: Insulin-degrading enzymes of mammals and bacteria / Andrew B. Becker, Richard A. Roth -- N-arginine dibasic convertase / Paul Cohen, Adrian R. Pierotti, Val�erie Chesneau, Thierry Foulon, Annik Prat -- Purification and characterization of mitochondrial processing peptidase of Neurospora crassa / Michael Brunner, Walter Neupert -- O-sialoglycoprotease from Pasteurella haemolytica / Alan Mellors, Reggie Y.C. Lo -- �I²-lytic endopeptidases / Efrat Kessler -- Procollagen N-peptidases: Procollagen N-proteinases / Karl E. Kadler, Samantha J. Lightfoot, Rod B. Watson -- Procollagen C-peptidase: Procollagen C-proteinase / Karl E. Kadler, Rod B. Watson -- Peptidyl-asp metalloendopeptidase / Marie-Luise Hagmann, Ursula Geuss, Stephan Fischer, Georg-Burkhard Kresse. | |
650 | 0 | |a Peptidase. | |
650 | 0 | |a Aspartic proteinases. | |
650 | 0 | |a Metalloproteinases. | |
650 | 1 | 2 | |a Aspartic Acid Endopeptidases |0 (DNLM)D016282 |
650 | 1 | 2 | |a Metalloendopeptidases |0 (DNLM)D008666 |
650 | 2 | |a Peptide Hydrolases |0 (DNLM)D010447 | |
650 | 2 | |a Metalloproteases |0 (DNLM)D045726 | |
650 | 6 | |a Peptidases. |0 (CaQQLa)201-0032233 | |
650 | 6 | |a Endopeptidases aspartiques. |0 (CaQQLa)201-0066908 | |
650 | 6 | |a M�etalloprot�einases. |0 (CaQQLa)201-0263781 | |
650 | 6 | |a M�etalloendopeptidases. |0 (CaQQLa)201-0419270 | |
650 | 7 | |a Aspartic proteinases |2 fast |0 (OCoLC)fst00818786 | |
650 | 7 | |a Metalloproteinases |2 fast |0 (OCoLC)fst01017929 | |
650 | 7 | |a Peptidase |2 fast |0 (OCoLC)fst01057550 | |
650 | 7 | |a Aspartatproteasen |2 gnd |0 (DE-588)4290183-2 | |
650 | 7 | |a Metalloenzym |2 gnd |0 (DE-588)4198095-5 | |
650 | 7 | |a Proteasen |2 gnd |0 (DE-588)4047521-9 | |
650 | 1 | 7 | |a Proteolyse. |2 gtt |
650 | 1 | 7 | |a Metalloprote�inases. |2 gtt |
650 | 1 | 7 | |a Asparaginezuur. |2 gtt |
650 | 1 | 7 | |a Peptidasen. |2 gtt |
650 | 1 | 7 | |a Enzymen. |2 gtt |
650 | 7 | |a Enzymologia |v podr�eczniki laboratoryjne. |2 jhpk | |
650 | 7 | |a Peptydazy. |2 jhpk | |
653 | 0 | |a Enzymes | |
700 | 1 | |a Barrett, Alan J., |e editor. | |
776 | 0 | 8 | |i Print version: |t Proteolytic enzymes. |d San Diego : Academic Press, �1995 |z 0121821498 |w (OCoLC)32730546 |
830 | 0 | |a Methods in enzymology ; |v v. 248. |x 0076-6879 | |
856 | 4 | 0 | |u https://sciencedirect.uam.elogim.com/science/book/9780121821494 |z Texto completo |
856 | 4 | 0 | |u https://sciencedirect.uam.elogim.com/science/bookseries/00766879/248 |z Texto completo |
880 | 0 | |6 505-00/(S |a Peptide thioester substrates for serine peptidases and metalloendopeptidases / James C. Powers, Chih-Min Kam -- Fluorimetric assays of proteolytic enzymes / C. Graham Knight -- Defined substrate mixtures for mapping of proteinase specificities / Gerard M. McGeehan, D. Mark Bickett, Jeffrey S. Wiseman, Michael Green, Judd Berman -- Assay of proteoglycan degradation / Christopher J. Handley, David J. Buttle -- Theoretical and practical aspects of proteinase inhibition kinetics / Joseph G. Bieth -- Active-site titration of peptidases / C. Graham Knight -- Families of aspartic peptidases, and those of unknown catalytic mechanism / Neil D. Rawlings, Alan J. Barrett -- Procathepsin E and cathepsin E / Takashi Kageyama -- Processing enzymes of pepsin family: Yeast aspartic protease 3 and pro-opiomelanocortin converting enzyme / Y. Peng Loh, Niamh X. Cawley -- Proteinase A from Aspergillus niger / Kenji Takahashi -- Thermopsin / Xinli Lin, Jordan Tang -- Bacterial prolipoprotein signal peptidase / Krishnan Sankaran, Henry C. Wu -- Evolutionary families of metallopeptidases / Neil D. Rawlings, Alan J. Barrett -- Removal and replacement of metal ions in metallopeptidases / David S. Auld -- Pseudolysin and other pathogen endopeptidases of thermolysin family / Kazuyuki Morihara -- Neprilysin: Assay methods, purification, and characterization / Chingwen Li, Louis B. Hersh -- Inhibitors of neprilysin: Design, pharmacological and clinical applications / Bernard P. Roques, Florence Noble, Philippe Crine, Marie-Claude Fourni�e-Zaluski -- Peptidyl dipeptidase A: Angiotensin I-converting enzyme / Pierre Corvol, Tracy A. Williams, Florent Soubrier -- Astacin / Walter St�ocker, Robert Zwilling -- Meprins A and B / Russell L. Wolz, Judith S. Bond -- Snake venom metalloendopeptidases: Reprolysins / J�on B. Bjarnason, Jay W. Fox -- Atrolysins: Metalloproteinases from Crotalus atrox venom / Jay W. Fox, J�on B. Bjarnason -- Membrane-associated metalloproteinase recognized by characteristic cleavage of myelin basic protein: Assay and isolation / Linda Howard, Paul Glynn -- Serralysin and related bacterial proteinases / Hiroshi Maeda, Kazuyuki Morihara -- Vertebrate collagenases / Marianna Dioszegi, Paul Cannon, Harold E. Van Wart -- Human neutrophil collagenase / Harald Tschesche -- Human stromelysins 1 and 2 / Hideaki Nagase -- Gelatinases A and B / Gillian Murphy, Thomas Crabbe -- Matrilysin / J. Frederick Woessner Jr. -- Tissue inhibitors of matrix metalloendopeptidases / Gillian Murphy, Frances Willenbrock -- Quantification of matrix metalloproteinases in tissue samples / J. Frederick Woessner Jr. -- Thimet oligopeptidase and oligopeptidase M or neurolysin / Alan J. Barrett, Molly A. Brown, Pamela M. Dando, C. Graham Knight, Norman McKie, Neil D. Rawlings, Atsushi Serizawa -- Mitochondrial intermediate peptidase / Grazia Isaya, Frantisek Kalousek -- Dipeptidyl carboxypeptidase and oligopeptidase A from Escherichia coli and Salmonella typhimurium / Christopher A. Conlin, Charles G. Miller -- Oligopeptidases from Lactococcus lactis / V�eronique Monnet -- Neurolysin: Purification and assays / F. Checler, H. Barelli, P. Dauch, V. Dive, B. Vincent, J.P. Vincent -- Leishmanolysin: Surface metalloproteinase of Leishmania / Jacques Bouvier, Pascal Schneider, Robert Etges -- Immunoglobulin A-metallo-type specific prolyl endopeptidases / Andrew G. Plaut, Andrew Wright -- Tetanus and botulism neurotoxins: Isolation and assay / Giampietro Schiavo, Cesare Montecucco -- Human carboxypeptidase N: Lysine carboxypeptidase / Randal A. Skidgel -- Human carboxypeptidase M / Fulong Tan, Peter A. Deddish, Randal A. Skidgel -- Carboxypeptidase T / Valentin M. Stepanov -- Pitrilysin / Angela Anastasi, Alan J. Barrett -- Insulysin and pitrilysin: Insulin-degrading enzymes of mammals and bacteria / Andrew B. Becker, Richard A. Roth -- N-arginine dibasic convertase / Paul Cohen, Adrian R. Pierotti, Val�erie Chesneau, Thierry Foulon, Annik Prat -- Purification and characterization of mitochondrial processing peptidase of Neurospora crassa / Michael Brunner, Walter Neupert -- O-sialoglycoprotease from Pasteurella haemolytica / Alan Mellors, Reggie Y.C. Lo -- β-lytic endopeptidases / Efrat Kessler -- Procollagen N-peptidases: Procollagen N-proteinases / Karl E. Kadler, Samantha J. Lightfoot, Rod B. Watson -- Procollagen C-peptidase: Procollagen C-proteinase / Karl E. Kadler, Rod B. Watson -- Peptidyl-asp metalloendopeptidase / Marie-Luise Hagmann, Ursula Geuss, Stephan Fischer, Georg-Burkhard Kresse. |