Proteins

1. Front Matter

   Pages i-xii

   PDF

2. The Lowry Method for Protein Quantitation

   • Jaap H. Waterborg, Harry R. Matthews

   Pages 1-3

3. Determination of Protein Molecular Weights by Gel Permeation High Pressure Liquid Chromatography

   • E. L. V. Mayes

   Pages 5-12

4. Immunoaffinity Purification of Protein Antigens

   • E. L. V. Mayes

   Pages 13-20

5. Electrophoretic and Chromatographic Separation of Peptides on Paper

   • E. L. V. Mayes

   Pages 21-32

6. Peptide Mapping by Reverse-Phase High Pressure Liquid Chromatography

   • E. L. V. Mayes

   Pages 33-39

7. SDS Polyacrylamide Gel Electrophoresis of Proteins

   • B. J. Smith

   Pages 41-55

8. Gradient SDS Polyacrylamide Gel Electrophoresis

   • John M. Walker

   Pages 57-61

9. Acetic Acid-Urea Polyacrylamide Gel Electrophoresis of Proteins

   • B. J. Smith

   Pages 63-73

10. The In Vivo Isotopic Labeling of Proteins for Polyacrylamide Gel Electrophoresis

    • Jeffrey W. Pollard

    Pages 75-80

11. Two-Dimensional Polyacrylamide Gel Electrophoresis of Proteins

    • Jeffrey W. Pollard

    Pages 81-96

12. Starch Gel Electrophoresis of Proteins

    • Graham B. Divall

    Pages 97-104

13. Isoelectric Focusing in Ultrathin Polyacrylamide Gels

    • Graham B. Divall

    Pages 105-111

14. High-Sensitivity Silver Staining of Proteins Following Polyacrylamide Gel Electrophoresis

    • Keith Gooderham

    Pages 113-118

15. Quantification of Proteins on Polyacrylamide Gels (Nonradioactive)

    • B. J. Smith

    Pages 119-125

16. Computer Analysis of Gel Scans

    • Harry R. Matthews

    Pages 127-139

17. Drying Gels

    • Bryan J. Smith

    Pages 141-146

18. Fluorography of Polyacrylamide Gels Containing Tritium

    • Jaap H. Waterborg, Harry R. Matthews

    Pages 147-152

19. Recovery of Proteins from Dried Polyacrylamide Gels after Fluorography

    • Jaap H. Waterborg, Harry R. Matthews

    Pages 153-155

20. The Electrophoretic Elution of Proteins from Polyacrylamide Gels

    • Jaap H. Waterborg, Harry R. Matthews

    Pages 157-164

In recent years there has been a tremendous increase in our understanding of the functioning of the cell at the molecular level. This has been achieved in the main by the invention and development of new methodology, parti- larly in that area generally referred to as "'genetic en- neering". While this revolution has been taking place in the field of nucleic acids research, the protein chemist has at the same time developed fresh methodology to keep pace with the requirements of present day molecular bi- ogy. Today's molecular biologist can no longer be content with being an expert in one particular area alone. He/she needs to be equally competent in the laboratory at h- dling DNA, RNA, and proteins, moving from one area to another as required by the problem he/she is trying to solve. Although many of the new techniques in molecular biology are relatively easy to master, it is often difficult for a researcher to obtain all the relevant information nec- sary for setting up and successfully applying a new te- nique. Information is of course available in the research l- erature, but this often lacks the depth of description that the new user requires. This requirement for in-depth pr- tical details has become apparent by the considerable - mand for places on our Molecular Biology Workshops held at Hatfield each summer.

• School of Biological and Environmental Sciences, The Hatfield Polytechnic, Hatfield, England

  John M. Walker

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