Comparison of two techniques for protein isolation and radioiodination by tryptic peptide mapping
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference16 articles.
1. Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis.
2. Radioiodination of proteins in single polyacrylamide gel slices. Tryptic peptide analysis of all the major members of complex multicomponent systems using microgram quantities of total protein.
3. Polymorphism of the major envelope glycoprotein (gp70) of murine C-type viruses: virion associated and differentiation antigens encoded by a multi-gene family
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2. Differences of nucleoproteins of human and avian influenza a virus strains shown by polyacrylamide gel electrophoresis and by the peptide mapping technique;Archives of Virology;1986-09
3. Immune-mapping as a specific and sensitive probe for the characterization of proteins;Biochemical Society Transactions;1985-04-01
4. Turnover and orientation of the major neural retina cell surface protein protected from tryptic cleavage by calcium;Biochemistry;1984-02-28
5. Phaseolus vulgaris cytoplasmic leucyl-tRNA synthetase. Purification and comparison of its catalytic, structural, and immunological properties with those of the chloroplastic enzyme.;Journal of Biological Chemistry;1983-10
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