rdf-syntax-grammar
mods:
  schema location: http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-2.xsd
  title info:
    title: Handbook of Proteolytic Enzymes
  name:
    name part: Salvesen, Guy
    role:
      role term: creator
    role:
      role term: Editor-In-Chief.
    role:
      role term: oth
  name:
    name part: Rawlings, Neil D.
    role:
      role term: Editor-In-Chief.
    role:
      role term: oth
  name:
    name part: ScienceDirect (Online service)
  type of resource: text
  genre: Electronic books.
  genre: Handbooks and manuals
  origin info:
    place:
      place term: mou
    place:
      place term: San Diego
    publisher: Academic Press [Imprint]
    publisher: Elsevier Science & Technology Books.
    date issued: 2012
    edition: 3rd ed.
    issuance: monographic
  language:
    language term: eng
  physical description:
    form: remote
    extent: 1 online resource (4094 p. :) ill.
  abstract: The third edition of the Handbook of Proteolytic Enzymes is a comprehensive reference work for the enzymes that cleave proteins and peptides, written by acknowledged experts in the field and containing over 850 chapters. Each chapter is organized into sections describing the name and history, activity and specificity, structural chemistry, preparation, biological aspects, and distinguishing features for a specific peptidase. There are also introductory chapters on peptidase classification and mechanisms and a comprehensive index. For the first time, the Handbook is also available online via Elsevier's ScienceDirect platform as well as a three-volume book. The online version has enhanced options, including online multimedia, cross-referencing capabilities, integrated online delivery and closer integration with the online MEROPS database of peptidases and their inhibitors. This reference work is a must-have for biochemists, biotechnologists, molecular biologists and students in these disciplines, and will be of great interest to pharmaceutical and biotechnology companies. Contains over 830 chapters Covers new research in therapeutics and drug trials Supplies content written by experts in the field.
  table of contents: E9780123822192v1.pdf -- Front Cover -- Handbook of Proteolytic Enzymes, Volume 1 -- Copyright Page -- Contents -- Editor Biographies -- Contributors -- Preface -- Introduction -- Terminology -- Organization of the Handbook -- Special forms of information in the Handbook -- Links to the MEROPS database -- Molecular images -- Alignments -- Secondary structure -- Description of substrate specificity -- References -- Aspartic Peptidases -- 1 Introduction: Aspartic and Glutamic Peptidases and Their Clans -- Clan AA -- Family A1 -- Other Families in Clan AA -- Clan AF -- Clan AC -- Clan AD -- Clan AE -- Other Families -- Glutamic Peptidases -- Asparagine Peptide Lyases -- Clans NA, NC and NE -- Inteins -- Autotransporters -- References -- 2 Catalytic Pathways of Aspartic Peptidases -- Introduction -- Enzymatic Mechanism of Aspartic Peptidases -- Enzymatic Mechanism of Glutamic Peptidases -- References -- 3 Pepsin A -- Databanks -- Name and History -- Activity and Specificity -- Structural Chemistry -- Pepsinogen -- Preparation -- Biological Aspects -- Related Peptidases -- Further Reading -- References -- 4 Pepsin B -- Databanks -- Name and History -- Activity and Specificity -- Structural Chemistry -- Preparation -- Biological Aspects -- Further Reading -- References -- 5 Chymosin -- Databanks -- Name and History -- Activity and Specificity -- Structural Chemistry -- Preparation -- Biological Aspects -- Distinguishing Features -- Related Proteinases -- Further Reading -- References -- 6 Cathepsin E -- Databanks -- Name and History -- Activity and Specificity -- Structural Chemistry -- Preparation -- Biological Aspects -- Tissue Distribution and Subcellular Localization -- Regulation of Gene Expression -- Processing, Maturation and Intracellular Trafficking Of Cathepsin E -- Physiological Roles of Cathepsin E -- Distinguishing Features.
  table of contents: Further Reading -- References -- 7 Gastricsin -- Databanks -- Name and History -- Activity and Specificity -- Structural Chemistry -- Progastricsin -- Preparation -- Biological Aspects -- References -- 8 Cathepsin D -- Databanks -- Name and History -- Activity and Specificity -- Assay Methods -- Specificity -- Inhibition and Activation -- Structural Chemistry -- Three-dimensional Structure -- Preparation -- Biological Aspects -- Gene and Expression Control -- Knock-out Model -- Organ Distribution and Cellular Localization -- Apoptosis -- Involvement in Cancer -- Neurodegeneration -- Other Biological Functions -- Distinguishing Features -- Related Peptidases -- Acknowledgment -- Further Reading -- References -- 9 Nothepsin -- Databanks -- Name and History -- Activity and Specificity -- Structural Chemistry -- Primary Structure Analysis -- Distinguishing Features of This New Class of Aspartic Proteinases -- Retrieval and Sequencing of Nothepsin Enzymes -- Presence of a Nothepsin Enzyme in Non-Antarctic Fish -- Nothepsin in Organisms Other Than Fish -- Preparation -- Biological Aspects -- Expression Pattern of the Nothepsin in Fish and Lizard -- Phylogenetic Analysis, Adaptive Evolution and Role of Nothepsin -- Further Reading -- References -- 10 Napsin A -- Databanks -- Name and History -- Activity and Specificity -- Structural Chemistry -- Preparation -- Biological Aspects -- Further Reading -- References -- 11 Renin -- Databanks -- Name and History -- Activity and Specificity -- Structural Chemistry -- Preparation -- Biological and Molecular Aspects -- Summary and Future Perspective -- Further Reading -- References -- 12 Mouse Submandibular Renin -- Databanks -- Name and History -- Activity and Specificity -- Structural Chemistry -- Preparation -- Biological Aspects -- Distinguishing Features -- References -- 13 Memapsin 1 -- Databanks.
  table of contents: Name and History -- Activity and Specificity -- Reaction and Specificity -- Assay Methods -- Enzymic Properties -- Inhibitors -- Structural Chemistry -- Preparation -- Biological Aspects -- Related Peptidases -- References -- 14 Memapsin 2 -- Databanks -- Name and History -- Activity and Specificity -- Reaction and Specificity -- Assay Methods -- Enzymic Properties -- Inhibitors -- Structural Chemistry -- Preparation -- Biological Aspects -- Related Peptidases -- Further Reading -- References -- 15 Pregnancy-Associated Glycoproteins -- Databanks -- Name and History -- Activity and Specificity -- Structural Chemistry -- Preparation -- Biological Aspects -- Distinguishing Features -- Further Reading -- References -- 16 Pepsin F -- Databanks -- Name and History -- Activity and Specificity -- Structural Chemistry -- Preparation -- Biological Aspects -- Distinguishing Features -- Further Reading -- References -- 17 Food Vacuole Plasmepsins -- Databanks -- Name and History -- Activity and Specificity -- Structural Chemistry -- Preparation -- Biological Aspects -- Distinguishing Features -- Related Peptidases -- Further Reading -- References -- 18 Plasmepsin V -- Databanks -- Name and History -- Activity and Specificity -- Structural Chemistry -- Preparation -- Biological Aspects -- Distinguishing Features -- Related Peptidases -- Further Reading -- References -- 19 Histo-Aspartic Proteinase -- Databanks -- Name and History -- Activity and Specificity -- Structural Chemistry -- Preparation -- Biological Aspects -- Distinguishing Features -- Related Peptidases -- References -- 20 Tick Heme-Binding Aspartic Proteinase -- Databanks -- Name and History -- Activity and Specificity -- Structural Chemistry -- Preparation -- Biological Aspects -- Distinguishing Features -- Further Reading -- References -- 21 Yolk Cathepsin (Boophilus sp.) -- Databanks.
  table of contents: Name and History -- Activity and Specificity -- Structural Chemistry and Preparation -- Biological Aspects -- Distinguishing Features -- Further Reading -- References -- 22 Na-APR-1 (aka Necepsin-2) -- Databanks -- Name and History -- Discovery -- Synonyms and Historic Name -- Activity and Specificity -- Reaction and Specificity -- Proteolysis of Hemoglobin -- Proteolysis of Fluorogenic Substrates -- Inhibitors -- Structural Chemistry -- Primary Structure and Secondary Structure -- Tertiary Structure -- Preparation -- Source (Biological/Commercial) -- Expression Systems -- Isolation, Purification and Refolding -- Biological Aspects -- Immunolocalization in Adult Stage Hookworms -- Neutralization of Proteolysis -- Aspartic Protease as a Potential Hookworm Vaccine -- Distinguishing Features -- Related Peptidases -- Further Reading -- References -- 23 Phytepsin -- Databanks -- Name and History -- Activity and Specificity -- Structural Chemistry -- Primary Structure -- Tertiary Structure -- Preparation -- Biological Aspects -- Proenzyme Activation -- Intracellular Transport -- Distribution in Tissues and Function -- Acknowledgments -- Further Reading -- References -- 24 Nepenthesin -- Databanks -- Name and History -- Activity and Specificity -- Structural Chemistry -- Preparation -- Biological Aspects -- Distinguishing Features -- Related Peptidases -- Further Reading -- References -- 25 Saccharopepsin -- Databanks -- Name and History -- Activity and Specificity -- Active Site -- Inhibition -- Structural Chemistry -- Preparation -- Biological Aspects -- Distinguishing Features -- Other Uses -- Related Peptidases -- Further Reading -- References -- 26 Acrocylindropepsin -- Databanks -- Name and History -- Activity and Specificity -- Structural Chemistry -- Preparation -- Biological Aspects -- Distinguishing Features -- Related Peptidases -- References.
  table of contents: 27 Aspergillopepsin I -- Databanks -- Name and History -- Activity and Specificity -- Structural Chemistry -- Preparation -- Biological Aspects -- Economic Features -- Distinguishing Features -- Related Peptidases -- Further Reading -- References -- 28 Penicillopepsin -- Databanks -- Name and History -- Activity and Specificity -- Structural Chemistry -- Preparation -- Biological Aspects -- Distinguishing Features -- Related Enzymes -- Penicillopepsin-JT2 and -JT3 -- Penicillopepsin from Penicillium Roqueforti -- Penicillopepsin from Penicillium duponti -- Penicillopepsin from Penicillium camemberti -- References -- 29 Endothiapepsin -- Databanks -- Name and History -- Activity and Specificity -- Structural Chemistry -- Preparation -- Biological Aspects -- Further Reading -- References -- 30 Rhizopuspepsin -- Databanks -- Name and History -- Activity and Specificity -- Structural Chemistry -- Preparation -- Biological Aspects -- Related Peptidases -- References -- 31 Mucorpepsin -- Databanks -- Name and History -- Activity and Specificity -- Structural Chemistry -- Preparation -- Biological Aspects -- Further Reading -- References -- 32 Polyporopepsin -- Databanks -- Name and History -- Activity and Specificity -- Structural Chemistry -- Preparation -- Biological Aspects -- Distinguishing Features -- Further Reading -- References -- 33 Candidapepsin -- Databanks -- Name and History -- Activity and Specificity -- Structural Chemistry -- Preparation -- Biological Aspects -- Distinguishing Features -- Related Peptidases -- Further Reading -- References -- 34 Candidaparapsin -- Databanks -- Name and History -- Activity and Specificity -- Structural Chemistry -- Preparation -- Biological Aspects -- Distinguishing Features -- Related Peptidases -- Further Reading -- References -- 35 Canditropsin -- Databanks -- Name and History -- Activity and Specificity.
  target audience: Scholarly & Professional Elsevier Science & Technology Books.
  subject:
    topic: Proteolytic enzymes
    genre: Handbooks, manuals, etc
  subject:
    topic: Proteolytic enzymes
  subject:
    topic: Proteolytic Enzymes
  subject:
    topic: Medical
    topic: Biochemistry
  subject:
    topic: Enzymes protéolytiques
    genre: Guides, manuels, etc
  subject:
    topic: Enzymes protéolytiques
  subject:
    topic: Proteolytic enzymes
  classification: QP609.P78
  classification: 572.76
  identifier: 9780123822192
  identifier: 012382219X
  identifier: 00991439
  identifier: http://proxy.library.tamu.edu/login
  record info:
    record content source: VT2
    record creation date: 110706
    record change date: 20260327165829.5
    record identifier: in00005767680
    language of cataloging:
      language term: eng