Purification and characterization of E37, a major chloroplast envelope protein.
We have purified to homogeneity E37, the second major polypeptide of the inner membrane of the chloroplast envelope. The protein was retained on a Mono S column at pH 7, indicating it is a basic protein. After cyanogen cleavage, the protein was partially sequenced at 2 different sites. The sequence is compared with the deduced amino acid sequence of a cDNA coding for a 37 kDa envelope polypeptide recently published by Dreses-Werringloer et al. (Eur. J. Biochem. (1991) 195, 361-368.)
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DBMS/PCV, UA no. 576 au CNRS, CENG et UJF 85X, Grenoble, France.
Joyard
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Douce
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D000595:Amino Acid Sequence; D060365:Chloroplast Proteins; D002736:Chloroplasts / Q000737:chemistry* / Q000648:ultrastructure; D002852:Chromatography, Ion Exchange; D003488:Cyanogen Bromide; D004591:Electrophoresis, Polyacrylamide Gel; D015151:Immunoblotting; D007425:Intracellular Membranes / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D010940:Plant Proteins / Q000737:chemistry / Q000302:isolation & purification*; D010944:Plants / Q000648:ultrastructure
D060365:Chloroplast Proteins; D008565:Membrane Proteins; D010446:Peptide Fragments; D010940:Plant Proteins; D003488:Cyanogen Bromide