In situ chemical cleavage of proteins immobilized to glass-fiber and polyvinylidenedifluoride membranes: Cleavage at tryptophan residues with 2-(2′-nitrophenylsulfenyl)-3-methyl-3′-bromoindolenine to obtain internal amino acid sequence-Reference-Cited by-同舟云学术

In situ chemical cleavage of proteins immobilized to glass-fiber and polyvinylidenedifluoride membranes: Cleavage at tryptophan residues with 2-(2′-nitrophenylsulfenyl)-3-methyl-3′-bromoindolenine to obtain internal amino acid sequence

Published:1990-05 Issue:1 Volume:187 Page:27-38
ISSN:0003-2697
Container-title:Analytical Biochemistry
language:en
Short-container-title:Analytical Biochemistry

Author:

Crimmins Dan L.,McCourt David W.,Thoma Richard S.,Scott Mitchell G.,Macke Kimberly,Schwartz Benjamin D.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference28 articles.

1. A gas-liquid solid phase peptide and protein sequenator.

2. Electroblotting onto activated glass. High efficiency preparation of proteins from analytical sodium dodecyl sulfate-polyacrylamide gels for direct sequence analysis.

3. Covalent immobilization of proteins for high-sensitivity sequence analysis: electroblotting onto chemically activated glass from sodium dodecyl sulfate-polyacrylamide gels

4. Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes.

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