Harald Tschesche 
Review Articles, including those from an International Conference held in Bielefeld, F. R. of Germany, June 1–2, 1984 [PDF ebook] 

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Frontmatter — CONTENTS — MODERN MICROMETHODS — CHROMOGENIC PEPTIDE SUBSTRATES FOR THE DETERMINATION OF SERINE PROTEASES. A BRIEF REVIEW. — IMMOBILIZED METAL ION AFFINITY CHROMATOGRAPHY – A POWERFUL METHOD FOR PROTEIN PURIFICATION — USE OF SYNTHETIC DYES FOR AFFINITY CHROMATOGRAPHY OF PROTEINS — FLUORESCENCE-ACTIVATED CELL SORTING: ISOLATION OF GENETIC VARIANTS FOR THE ANALYSIS OF PROTEIN STRUCTURE AND FUNCTION — THE FPLC*-SYSTEM FOR FAST AND HIGH RESOLUTION SEPARATIONS OF PROTEINS — AMINO ACID ANALYSIS BY HIGH PERFORMANCE LIQUID CHROMATOGRAPHY AND PRECOLUMN DERIVATISATION — POTENTIALS OF HIGH-PERFORMANCE ION-EXCHANGE CHROMATOGRAPHY IN PROTEIN SEPARATIONS – — SEPARATION OF CYANOGEN BROMIDE PEPTIDES OBTAINED FROM THE CATALYTIC DOMAIN OF THE NADPH-CYTOCHROME P-450 REDUCTASE (PIG LIVER) BY HPLC ON WIDE PORE COLUMN — IMMUNOASSAYS OF PEPTIDES AND PROTEINS — CHEMICAL MODIFICATION OF PROTEINS — CROSS-LINKING REAGENTS — MICRO-ANALYSIS OF POLYPEPTIDE STRUCTURE USING COLOR REAGENTS — A MODULAR SYSTEM FOR MICROSEQUENCING OF PROTEINS, OLIGONUCLEOTIDE SYNTHESIS AND PEPTIDE SYNTHESIS — ON-LINE DETECTION OF AMINO ACID DERIVATIVES RELEASED BY AUTOMATIC EDMAN DEGRADATION OF POLYPEPTIDES — PROGRAMMABLE ELECTRONIC CONTROL OF SEQUENTIAL PROCEDURES OF ANALYTICAL DEVICES — IMPROVED ISOCRATIC SEPARATION OF PHENYLTHIOHYDANTOIN AMINO ACIDS DOWN TO THE FEMTOMOLE LEVEL — APPLICATION OF COMPUTER PROGRAMS FOR THE STRUCTURAL ANALYSIS OF PROTEINS — DNA AND RNA SEQUENCE ANALYSIS — SECONDARY STRUCTURE DETERMINATION OF MEMBRANE PROTEINS BY RAMAN SPECTROSCOPY — STANDARD METHODS FOR THE CHEMICAL SYNTHESIS OF PEPTIDES — AUTHOR INDEX — SUBJECT INDEX

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Dil İngilizce ● Biçim PDF ● Sayfalar 443 ● ISBN 9783112393048 ● Dosya boyutu 80.1 MB ● Editör Harald Tschesche ● Yayımcı De Gruyter ● Kent Berlin/Boston ● Yayınlanan 2021 ● Baskı 1 ● İndirilebilir 24 aylar ● Döviz EUR ● Kimlik 8519585 ● Kopya koruma Adobe DRM
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