Literature DB >> 3178813

A simple in situ cyanogen bromide cleavage method to obtain internal amino acid sequence of proteins electroblotted to polyvinyldifluoride membranes.

M G Scott1, D L Crimmins, D W McCourt, J J Tarrand, M C Eyerman, M H Nahm.   

Abstract

We report a simple method to obtain internal amino acid sequences from larger proteins electroblotted to polyvinyldifluoride membranes. To demonstrate this method, immunoglobulin heavy and light chains are separated by gel electrophoresis and electroblotted to the membrane. The separated chains, immobilized to the membrane, are cleaved in situ by cyanogen bromide and the resulting fragments are subsequently eluted from the membrane. The fragments are separated by gel electrophoresis, electroblotted and subjected to gas-phase microsequence analysis.

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Year:  1988        PMID： 3178813     DOI： 10.1016/s0006-291x(88)81290-7

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN： 0006-291X            Impact factor:   3.575


  11 in total

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5.  Enantiomeric barbiturates bind distinct inter- and intrasubunit binding sites in a nicotinic acetylcholine receptor (nAChR).

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6.  Interaction of synthetic Alzheimer beta-protein-derived analogs with aqueous aluminum: a low-field 27Al NMR investigation.

Authors:  S B Vyas; L K Duffy
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8.  Positive and Negative Allosteric Modulation of an α1β3γ2 γ-Aminobutyric Acid Type A (GABAA) Receptor by Binding to a Site in the Transmembrane Domain at the γ+-β- Interface.

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9.  Multiple propofol-binding sites in a γ-aminobutyric acid type A receptor (GABAAR) identified using a photoreactive propofol analog.

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10.  Molecular cloning and sequencing of the cDNA and gene for a novel elastinolytic metalloproteinase from Aspergillus fumigatus and its expression in Escherichia coli.

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