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Mosby’s Diagnostic and Laboratory Test Reference 8e by Kathleen Deska Pagana, and Timothy J. Pagana Hardcover - 1,136 pages Shipped in CLICK HERE Cat.# EL-LABM1 $ 58.20 BUY Published:  2006   ISBN:  9780323046343

Mosby’s Diagnostic and Laboratory Test Reference is a comprehensive and up-to-date handbook that offers clinically-relevant information on laboratory and diagnostic tests. The test entries are organized alphabetically for quick reference. Tests are presented in a consistent format, which allows for concise coverage without sacrificing the depth of detail necessary for a thorough understanding of diagnostic
testing. Each test entry includes, where relevant: alternate or abbreviated test names; type of test; normal findings; possible critical values; test explanation and related physiology; contraindications; potential complications; interfering factors; procedure and patient care (before, during, and after); and abnormal findings. Related tests are extensively cross-referenced throughout the book. The book’s portable size and durable cover make it a handy on-the-spot reference.

Key Features:
1. Tests organized alphabetically with A-to-Z thumb tabs for quick reference.
2. Each test entry begins on a new page making tests easy to find.
3. Normal findings for adult (male and female), elderly, and pediatric patients are included where applicable to provide complete clinical data.
4. Possible critical values are highlighted to alert the reader to situations requiring immediate intervention.
5. Symbol next to drug-related interfering factors alerts the reader to the effects of pharmacologic agents on tests.
6. Icon for patient teaching-related care indicates information that should be shared with patients and their families.

Force Microscopy, Applications in Biology and Medicine by Bhanu P. Jena, and J. K. Heinrich Horber Hardcover - 300 pages Shipped in CLICK HERE Cat.# JW-LABM3 $156.30 BUY Published:  2006   ISBN:  9780471396284

A complete examination of the uses of the atomic force
microscope in biology and medicine

This cutting-edge text, written by a team of leading experts, is the first detailed examination of the latest, most powerful scanning probe microscope, the atomic force microscope (AFM). Using the AFM, in combination with conventional tools and techniques, readers gain a profound understanding of the cell, subcellular organelles, and biomolecular structure and function.

The text begins with three chapters describing the molecular machinery and mechanism of cell secretion and membrane fusion in cells, using approaches that combine AFM, electron microscopy, X-ray diffraction, photon correlation spectroscopy, molecular biology, biochemistry, and electrophysiology. The discovery of a new cellular structure the "porosome" or fusion pore--the cells secretory machinery, the molecular mechanism of membrane fusion in cells, and the expulsion of intravesicular contents during cell secretion are outlined in the first three chapters. The book also covers:

• Identification of the "porosome" in the growth hormone secreting cell of the pituitary gland
• Probing the structural and physical properties of microbial cell surfaces
• Scanning probe microscopic characterization of the higher plant cell wall and its components
• Case studies of nano drug delivery systems using engineered dendrimers
• AFM techniques for studying living cells
• Investigating the intermolecular forces of leukocyte adhesion molecules
• Protein-protein interactions
• Micromechanical properties of lipid bilayers and vesicles

The text concludes with four chapters that examine new and emerging approaches in the use of force microscopy in biology and medicine.

This text is ideal for advanced undergraduate and graduate students and researchers in cell and molecular biology, genetics, genomics, physiology, neuroscience, biophysics, and biochemistry. Not only does it provide the theory, but also practical considerations such as the selection of the right tools and approach.

Table of Contents:

Preface
Contributors

Chapter 1. Porosome: The Universal Secretory Machinery in Cells
Chapter 2. Molecular Mechanism of SNARE-Induced Membrane Fusion
Chapter 3. Molecular Mechanism of Secretory Vesicle Content Expulsion During Cell Secretion
Chapter 4. Fusion Pores in Growth-Hormone-Secreting Cells of the Pituitary Gland: An AFM Study
Chapter 5. Properties of Microbial Cell Surfaces Examined by Atomic Force Microscopy
Chapter 6. Scanning Probe Microscopy of Plant Cell Wall and Its Constituents
Chapter 7. Cellular Interactions of Nano Drug Delivery Systems
Chapter 8. Adapting AFM Techniques for Studies on Living Cells
Chapter 9. Intermolecular Forces of Leukocyte Adhesion Molecules
Chapter 10. Mechanisms of Avidity Modulation in Leukocyte Adhesion Studied by AFM
Chapter 11. Resolving the Thickness and Micromechanical Properties of Lipid Bilayers and Vesicles Using AFM
Chapter 12. Imaging Soft Surfaces by SFM
Chapter 13. High-Speed Atomic Force Microscopy of Biomolecules in Motion
Chapter 14. Atomic Force Microscopy in Cytogenetics
Chapter 15. Atomic Force Microscopy in the Study of Macromolecular Interactions in Hemostasis and Thrombosis: Utility for Investigation of the Antiphospholipid Syndrome

Index

Exploring the Human Plasma Proteome by Gilbert S. Omenn Hardcover - 394 pages Shipped in CLICK HERE Cat.# JW-LABM4 $233.60 BUY Published:  2006   ISBN:  9783527317578

On the cutting edge of medical diagnostics, plasma proteomics promises to generate a new wave of technologies to help identify many different diseases and disease risks.

Plasma and serum are the preferred non-invasive specimens to test normal individuals, at-risk groups, and patients for protein biomarkers discovered and validated to reflect physiological, pathological, and pharmacological phenotypes. These specimens present enormous challenges due to extreme complexity, huge dynamic range in protein concentrations, non-standardized methods of sample processing, and intra- and inter-individual variation from genetics, diet, smoking, hormones, and other sources. This book presents the major findings from the collaborative Plasma Proteome Project organized by the international Human Proteome Organization (HUPO). The chapters are drawn from a larger set of publications in the journal PROTEOMICS. This book provides a valuable foundation for development and applications of proteomics.

Table of Contents:

1. Overview of the HUPO Plasma Proteome Project: Results from the pilot phase with 35 collaborating laboratories and multiple analytical groups, generating a core dataset of 3020 proteins and a publicly-available database

1.1 Introduction
1.2 PPP reference specimens
1.3 Bioinformatics and technology platforms
1.3.1 Constructing a PPP database for human plasma and serum proteins
1.3.2 Analysis of confidence of protein identifications
1.3.3 Quantitation of protein concentrations
1.4 Comparing the specimens
1.4.1 Choice of specimen and collection and handling variables
1.4.2 Depletion of abundant proteins followed by fractionation of intact proteins
1.4.3 Comparing technology platforms
1.4.4 Alternative search algorithms for peptide and protein identification
1.4.5 Independent analyses of raw spectra or peaklists
1.4.6 Comparisons with published reports
1.4.7 Direct MS (SELDI) analyses
1.4.8 Annotation of the HUPO PPP core dataset(s)
1.4.9 Identification of novel peptides using whole genome ORF search
1.4.10 Identification of microbial proteins in the circulation
1.5 Discussion
1.6 References

2. Data management and preliminary data analysis in the pilot phase of the HUPO Plasma Proteome Project

2.1 Introduction
2.2 Materials and methods
2.2.1 Development of the data model
2.2.2 Data submission process
2.2.3 Design of the data repository
2.2.4 Receipt of the data
2.3 Inference from peptide level to protein level
2.4 Summary of contributed data
2.4.1 Cross-laboratory comparison, confidence of the identifications
2.5 False-positive identifications
2.6 Data dissemination
2.7 Discussion
2.8 Concluding remarks
2.9 Computer technologies applied
2.10 References

3. HUPO Plasma Proteome Project specimen collection and handling: Towards the standardization of parameters for plasma proteome samples

3.1 Introduction
3.2 Materials and methods
3.2.1 HUPO reference sample collection protocol
3.2.2 Differential peptide display
3.2.3 Stability studies and SELDI analysis
3.2.4 SDS-PAGE analysis for stability studies
3.2.5 2-DE for stability studies
3.2.6 SELDI-TOF analysis for protease inhibitor studies
3.2.7 2-DE for plasma protease inhibition studies
3.2.8 Tryptic digestion and protein identification for protease inhibition studies
3.2.9 Antibody microarray analysis using two-color rolling circle amplification
3.3 Results
3.3.1 Comparisons of specimen types
3.3.2 Evaluation of storage and handling conditions
3.3.3 Evaluations of the use of protease inhibitors
3.4 Discussion
3.4.1 Other pre-analytical variables and control considerations
3.4.2 Reference materials
3.5 Concluding remarks
3.6 References

4. Immunoassay and antibody microarray analysis of the HUPO Plasma Proteome Project reference specimens: Systematic variation between sample types and calibration of mass spectrometry data

4.1 Introduction
4.2 Materials and methods
4.2.1 Reference specimens
4.2.2 DB immunoassays
4.2.3 Antibody arrays at GNF
4.2.4 Antibody microarrays at MSI
4.2.5 Antibody microarrays at VARI
4.2.6 Retrieval and matching of IPI numbers for the analytes
4.3 Results
4.3.1 Antibody-based measurements of the HUPO reference specimens
4.3.2 Systematic variation between the preparation methods of the PPP reference specimens
4.3.3 Consistent alterations in specific protein abundances
4.3.4 Linkage of MS data and antibody-based measurements
4.4 Discussion
4.5 References

5. Depletion of multiple high-abundance proteins improves protein profiling capacities of human serum and plasma

5.1 Introduction
5.2 Materials and methods
5.2.1 Serum/plasma collection
5.2.2 MARS
5.2.3 Multiple affinity removal spin cartridge
5.2.4 Microscale solution IEF (MicroSol IEF) (ZOOM-IEF) fractionation
5.2.5 2-DE
5.2.6 LC-MS/MS
5.3 Results
5.3.1 Depletion of major proteins to enhance detection of lower abundance proteins
5.3.2 Evaluation of high-abundance protein removal using 2-DE
5.3.3 Specificity of major protein depletion
5.3.4 Impact of Top-6 protein depletion on detection of lower abundance proteins using 2-D gels
5.3.5 Combining Top-6 protein depletion with microSol IEF prefractionation and narrow pH range gels
5.3.6 Analysis of Top-6 depleted serum and plasma using protein array pixelation
5.4 Discussion
5.5 References

6. A novel four-dimensional strategy combining protein and peptide separation methods enables detection of low-abundance proteins in human plasma and serum proteomes

6.1 Introduction
6.2 Materials and methods
6.2.1 Materials
6.2.2 Top six protein depletion
6.2.3 MicroSol-IEF fractionation
6.2.4 Protein array pixelation
6.2.5 LC-ESI-MS/MS methods
6.2.6 Data analysis
6.3 Results and discussion
6.3.1 Protein array pixelation strategy
6.3.2 Optimization of protein array pixelation
6.3.3 Total analysis time for protein array pixelation of human plasma proteome
6.3.4 Systematic protein array pixelation of the human plasma proteome
6.3.5 Systematic protein array pixelation of the human serum proteome
6.3.6 Analyses of human plasma and serum proteomes using HUPO filter criteria
6.4 Concluding remarks
6.5 References.

7. A study of glycoproteins in human serum and plasma reference standards (HUPO) using multilectin affinity chromatography coupled with RPLC-MS/MS

7.1 Introduction
7.2 Materials and methods
7.2.1 Materials
7.2.2 Isolating glycoproteins using multilectin affinity columns
7.2.3 Analysis of glycoproteins on LC-LCQ MS
7.2.4 Analysis of glycoproteins on LC-LTQ MS
7.2.5 Protein database search
7.3 Results and discussion
7.3.1 Protein IDs from the plasma and serum samples
7.3.2 Comparison between serum and plasma glycoproteomes
7.3.3 Comparison of the glycoproteins present in the samples collected from three ethnic groups
7.4 Concluding remarks
7.5 References

8. Evaluation of prefractionation methods as a preparatory step for multidimensional based chromatography of serum proteins

8.1 Introduction
8.1.1 The HUPO Plasma Proteome Project (PPP) goals and the serum as a complex sample
8.1.2 The scope of this manuscript
8.2 Materials and methods
8.2.1 Depletion from serum albumin and antibodies
8.2.2 MudPIT and mass segmentation
8.2.3 Protein separation by SDS-PAGE
8.2.4 SCX separation of intact proteins followed by MudPIT
8.2.5 Liquid-phase IEF followed by MudPIT
8.2.6 Capillary RP-LC-MS/MS
8.2.7 MS data processing and peptide/protein identifications
8.3 Results
8.3.1 Comparisons between the prefractionation methods
8.3.2 Identification of different protein subsets
8.3.3 Proteins identified by only one prefractionation method
8.3.4 Different methods resulted in diverse peptide coverage
8.4 Discussion
8.4.1 Giving every peptide a chance
8.4.2 How to identify more of the marginal proteins
8.4.3 Clustering and comparing raw data
8.4.4 High throughput and ruggedness versus high sensitivity
8.4.5 The cost effectiveness of the different methods
8.5 Concluding remarks
8.6 References

9. Efficient prefractionation of low-abundance proteins in human plasma and construction of a two-dimensional map

9.1 Introduction
9.2 Materials and methods
9.2.1 Plasma sample preparation
9.2.2 Depletion of major abundance proteins with an immunoaffinity column
9.2.3 2-DE
9.2.4 Identification of proteins by MS
9.2.5 Fractionation of the plasma samples by FFE
9.2.6 LC-MS/MS
9.2.7 Bioinformatics
9.3 Results and discussion
9.3.1 2-DE map of human plasma devoid of high-abundance proteins
9.3.2 Expression of different anticoagulant-treated plasma
9.3.3 FFE/1-DE/nanoLC-MS/MS and 2-DE/MALDI-TOF
9.4 Concluding remarks
9.5 References

10. Comparison of alternative analytical techniques for the characterisation of the human serum proteome in HUPO Plasma Proteome Project

10.1 Introduction
10.2 Materials and methods
10.2.1 Materials
10.2.2 Human serum samples
10.2.3 Integrated strategy for characterising analytical approaches
10.2.4 Depletion of the highly abundant serum proteins by MARS
10.2.5 Desalting and concentrating the flow-through fractions by centrifugal ultrafiltration
10.2.6 Fractionation of depleted serum samples by anion-exchange HPLC
10.2.7 Protein fractionation by 2-D HPLC with nonporous RP-HPLC
10.2.8 The 2-DE strategy for the analysis of serum proteins
10.2.8.1 2-DE
10.2.8.2 In-gel digestion via automated workstation
10.2.8.3 Protein spot identification by MALDI-TOF-MS/MS
10.2.9 Shotgun strategy for the analysis of serum proteins
10.2.10 Protein fractionation strategy for the analysis of serum proteins
10.2.11 Offline shotgun strategy for the analysis of serum proteins
10.2.12 Optimised nanoRP-HPLC-nanoESI IT-MS/MS for the reanalysis of offline SCX-separated peptides (offline-nanospray strategy)
10.3 Integrated analysis of the whole data sets
10.3.1 Protein grouping analysis
10.3.2 Sequence clustering
10.4 Results and discussion
10.4.1 Depletion of the highly abundant serum proteins
10.4.2 The 2-DE strategy for the analysis of serum proteins
10.4.3 2-D HPLC fractionation for the analysis of serum proteins
10.4.4 Shotgun strategy for the analysis of serumproteins with online SCX
10.4.5 Shotgun strategy for the analysis of serumproteins with offline SCX
10.4.6 Offline SCX shotgun-nanospray strategy for the analysis of serum proteins
10.4.7 Comparison of the five strategies for the analysis of the human serum proteome
10.5 Concluding remarks
10.6 References

11. A proteomic study of the HUPO Plasma Proteome Project’s pilot samples using an accurate mass and time tag strategy

11.1 Introduction
11.2 Materials and methods
11.2.1 Human blood serum and plasma
11.2.2 Depletion of Igs and trypsin digestion
11.2.3 Peptide cleanup
11.2.4 Capillary RP-LC
11.2.5 IT-MS
11.2.6 SEQUEST identification of peptides
11.2.7 Putative mass and time tag database from SEQUESTresults
11.2.8 FT-ICR-MS
11.2.9 cLC-FT-ICR MS data analysis
11.2.10 OmniViz cluster and visual analysis
11.3 Results
11.3.1 PuMT tag database
11.3.2 Summary of peptide/protein identifications by AMT tags
11.3.3 Protein concentration estimates from ion current
11.3.4 Global protein analysis
11.4 Discussion
11.4.1 Application of FT-ICR MS as a proteomic technology bridge
11.4.2 Confidence in any MS-based proteomic approach
11.4.3 Peptide/protein redundancy
11.4.4 Identification sensitivity versus specificity
11.4.5 Throughput and differential analysis
11.5 References

12. Analysis of Human Proteome Organization Plasma Proteome Project (HUPOPPP) reference specimens using surface enhanced laser desorption/ionization-time of flight (SELDI-TOF) mass spectrometry: Multi-institution correlation of spectra and identification of biomarkers

12.1 Introduction
12.2 Materials and methods
12.2.1 Sample preparation
12.2.2 Sample preprocessing
12.2.3 Target (CM10) chip preparation and sample incubation
12.2.4 Scanning protocol
12.2.5 Data processing
12.2.6 Bioinformatics analysis of data and correlation coefficient matrix
12.2.7 Protein purification, SDS-PAGE analysis, and extraction of proteins
12.2.8 Peptide mass fingerprinting (PMF)
12.2.9 MS/MS analysis
12.2.10 Western blot analysis
12.3 Results
12.4 Discussion
12.5 References

13. An evaluation, comparison, and accurate benchmarking of several publicly available MS/MS search algorithms: Sensitivity and specificity analysis

13.1 Introduction
13.1.1 Heuristic algorithms
13.1.2 Probabilistic algorithms
13.2 Materials and methods
13.2.1 HUPO-PPP reference specimens
13.2.2 Sample preparation and MS analysis
13.2.3 Protein sequence databases
13.2.4 MS/MS database search strategy
13.2.5 Web interface for data validation, integration, and cross annotation
13.2.6 ROC curve generation
13.3 Results and discussion
13.3.1 Comparison of MS/MS search algorithms
13.4 Concluding remarks
13.5 References

14. Human Plasma Peptide Atlas

14.1 References

15. Do we want our data raw? Including binary mass spectrometry data in public proteomics data repositories

15.1 References

16. A functional annotation of subproteomes in human plasma

16.1 Introduction
16.2 Materials and methods
16.2.1 Coagulation pathway and protein interaction network analysis
16.2.2 Gene ontology annotations
16.2.3 Analysis of MS-derived data for identification of proteolytic events and post-translational modifications
16.3 Results and discussion
16.3.1 Bioinformatic analyses of the functional subproteomes
16.3.2 Proteins involved in the blood coagulation pathway
16.3.3 Proteins potentially derived from mononuclear phagocytes
16.3.4 Proteins involved in inflammation
16.3.5 Analyzing the peptide subproteome of human plasma
16.3.6 Liver related plasma proteins
16.3.7 Cardiovascular system related plasma proteins
16.3.8 Glycoproteins
16.3.9 DNA-binding proteins
16.3.10 Annotation through reanalysis of mass spectrometry data
16.4 Concluding remarks
16.5 References

17. Cardiovascular-related proteins identified in human plasma by the HUPO Plasma Proteome Project Pilot Phase

17.1 Introduction
17.1.1 HUPO Plasma Proteome Project pilot phase
17.1.2 Need for novel insights into cardiovascular disease
17.2 Materials and methods
17.3 Groups of cardiovascular-related proteins
17.3.1 Markers of inflammation and CVD
17.3.2 Vascular and coagulation proteins
17.3.3 Signaling proteins
17.3.4 Growth- and differentiation-associated proteins
17.3.5 Cytoskeletal proteins
17.3.6 Transcription factors
17.3.7 Channel and receptor proteins
17.3.8 Heart failure- and remodeling-related proteins
17.4 Functional analyses and implications
17.4.1 Organ specific cardiovascular-related proteins in plasma
17.4.2 Novel cardiovascular-related proteins identified in plasma
17.5 Methodology considerations
17.6 Conclusions and future directions
17.7 References

Microfluidic Applications in Biology: From Technologies to Systems Biology by Niels Lion, Joel S. Rossier, and Hubert H. Girault Hardcover - 360 pages Shipped in CLICK HERE Cat.# JW-LABM5 $217.25 BUY Published:  2006   ISBN:  9783527317615

Taken from the high-impact journal Electrophoresis, these research articles on microfluidics and its application in a range of biological fields are of high interest and now available to a new readership. Alongside several review articles, this volume represents a current overview of the latest research.

Table of Contents:

Chapter 1.On-line chemiluminescence detection for isoelectric focusing of heme proteins on microchips.
Chapter 2. A simple microfluidic system for efficient capillary electrophoretic separation and sensitive fluorimetric detection of DNA fragments using light-emitting diode and liquid-core waveguide techniques.
Chapter 3. Determination ob biochemical species on electrophoresis chips with an external contactless conductivity detector.
Chapter 4. In-channel indirect amperometric detection of nonelectroactive anions for electrophoresis on a poly(dimethylsiloxane) microchip.
Chapter 5. Coupling on-chip solid-phase extraction to electrospray mass spectrometry through an integrated electrospray tip.
Chapter 6. Electrospray interfacing of polymer microfluidics to MALDI-MS.
Chapter 7. Nanoliquid chromatography-mass spectrometry of oligosaccharides employing graphitized carbon chromatography on microchip with a high-accuracy mass analyzer.
Chapter 8. Chip electrospray mass spectrometry for carbohydrate analysis.
Chapter 9. Utility of lab-on-a-chip technology for high-throughput nucleic acid and protein analysis.
Chapter 10. Analysis of amino acids and proteins using a poly (methyl methacrylate) microfluidic system.
Chapter 11. Single cell manipulation, analytics, and label-free protein detection microfluidic devices for systems nanobiology.
Chapter 12. Fast immobilization of probe beads by dielectrophoresis-controlled adhesion in a versatile microfluidic platform for affinity assay.
Chapter 13. Droplet fusion by alternating current (AC) field electrocoalescence in microchannels.
Chapter 14. Microfluidic flow focusing: Drop size and scaling in pressure versus flow-rate-driven pumping.
Chapter 15. Aligning fast alternating current electroosmotic flow fields and characteristic frequencies with dielectrophoretic traps to achieve rapid bacteria detection.
Chapter 16. Dielectrophoresis induced clustering regimes of viable yeast cells.
Chapter 17. 3-D electrode designs for flow-through dielectrophoretic systems.
Chapter 18. Parallel mixing of photolithographically defined nanoliter volumes using elastomeric microvalve arrays.
Chapter 19. Method development and measurements of endogenous serine/threonine akt phosphorylation using capillary electrophoresis for systems biology.
Chapter 20. Comparison of a pump-around, a diffusion-driven, and a shear-driven system for the hybridization of mouse lung and testis total RNA on microarrays.
Chapter 21. Microfluidic devices for the analysis of apoptosis.
Chapter 22. Effect of iron restriction on outer membrane protein composition of pseudomonas strains studied by conventional and microchip electrophoresis.

Index.

Tissue Engineering: From Cell Biology to Artificial Organs by Will W. Minuth, Raimund Strehl, and Karl Schumacher Hardcover - 324 pages Shipped in CLICK HERE Cat.# JW-LABM6 $195.40 BUY Published:  2005   ISBN:  9783527311866

Comprehensive in its scope and illustrated in detail, this practical book provides a fundamental insight into the complex world of tissue development and artificial cell culture using tissue engineering.
The introductory chapters cover basic cell biology and cellular development as well as cell culture, with a main emphasis on ways of differentiating tissue and the critical evaluation of the properties of maturing tissue constructs. The authors also focus on the use of stem cells from the most varied sources in tissue engineering.

The whole is rounded off by an exceptionally wide-ranging glossary containing some 1,000 key words from the fields of cell biology, cell culture development and tissue engineering.

Table of Contents:

Preface

1. Developmental processes

2 Cells and Tissue
2.1 The Cell
2.2 Tissue Types
2.3 Relevance of the ECM
2.4 Emergence of Tissue
2.5 Regeneration

3 Classical Culture Methods.

3.1 History
3.2 First Cultures
3.3 Tissue Culture
3.4 Organ Culture

4. Tissue Engineering

4.1 Cell Therapies
4.2 Tissue Constructs
4.3 Organ Modules
4.4 Cosmetic Measures

5. Concepts of Tissue Creation

5.1 Sources
5.2 Stem Cells
5.3 Cells from Tissues
5.4 Matrices
5.5 Culture Methods for Tissue Engineering
5.6 Perfusion Culture

6. Maturation of Tissue Constructs

6.1 Primary and Secondary Contacts
6.2 Building Structures
6.3 Terminal Differentiation
6.4 Impact of the Culture Environment on the Development of Tissue
6.5 Step by Step
6.6 Tissue Functions after Implantation
6.7 The Three Steps of Tissue Development

7. Development of the Perfusion System Tissue Factory

7.1 Requirements of the Culture System
7.2 Artificial Interstitium
7.3 Smart Matrices
7.4 Optimal Housing for the Perfusion System
7.5 Supply of the Maturing Tissue with Medium
7.6 Synopsis

8. Ensuring Tissue Quality

8.1 Norms and Cell Biology
8.2 Evaluating Complexity
8.3 Expression Behavior
8.4 Suitability of a Scaffold
8.5 Hidden Heterogeneity
8.6 Investigating Cellular Ultrastructures
8.7 Functional Transfer
8.8 Quality Assurance
8.9 Implant–Host Interaction

9. Perspectives

10. Ethical Aspects

Glossary
Companies
Literature
Subject Index

The Science of Laboratory Diagnosis by John Crocker, and David Burnett Hardcover - 564 pages Shipped in CLICK HERE Cat.# JW-LABM7 $269.95 BUY Published:  2005   ISBN:  9780470859124

This fully revised and updated edition of The Science of Laboratory Diagnosis provides a concise description of all common laboratory tests available in medical practice with notes on their application, the accuracy of each test, the historical background to the adoption of various tests and their effectiveness in diagnosis.

• Well illustrated, with clear headings, tables, flow charts and pathology slides, most in full colour
• Provides an accessible reference book in which relevant information can be found easily
• Page design facilitates rapid assimilation of principles and key facts
• All the chapters have been updated and new material has been introduced to cover recently developed techniques, such as fluid-based cytology, telepathology and proteomics

The Science of Laboratory Diagnosis, Second Edition is an essential primary reference source for everyone working in a clinical laboratory. This book is essential reading for pathologists, biomedical scientists, medical laboratory scientific officers and all clinicians involved in laboratory research.

Reviews of the First Edition:

"The text is concise, wide-ranging and easy to digest. The ease of extraction of the important facts make it an ideal source of information for use in a variety of situations from the postgraduate examination to the clinical directors' board meeting." BULLETIN OF THE ROYAL COLLEGE OF PATHOLOGISTS

"The editors have done a marvellous job, more than fulfilling their stated aim of producing a volume describing the multidisciplinary state of modern pathology which will be of interest to a wide range of readers. … I was particularly impressed by the many tables and flow charts, which can be used as aids to decision making." JOURNAL OF CLINICAL PATHOLOGY

"This is an excellent book to dip into and get a feel for techniques used in the other disciplines of pathology.&qu