NDLI: Partial primary structure of bacteriorhodopsin: sequencing methods for membrane proteins.

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Partial primary structure of bacteriorhodopsin: sequencing methods for membrane proteins.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Biemann, K. Khorana, H. G. Gerber, G. E. Anderegg, R. J. Herlihy, W. C. Gray, C. P.
Abstract	The sequence of 102 amino acid residues from the NH2 terminus and that of 39 amino acid residues from the COOH terminus of bacteriorhodopsin have been determined. These results are in agreement with those recently published by Ovchinnikov and coworkers [Ovchinnikov, Y.A., Abdulaey, N.G., Feigina, M.Y., Kiselev, A.V. & Lobanov, N.A. (1977) FEBS Lett. 84, 1-4]. Chymotryptic cleavage of bacteriorhodopsin produced two fragments, C-1 (Mr 19,000) and C-2 (Mr 6900), the latter containing the blocked NH2 terminus (pyroglutamic acid). Further fragmentation with CNBr gave mostly hydrophobic fragments, which were separated by gel permeation and reverse-phase high-pressure liquid chromatography in formic acid/ethanol/water mixtures. The fragments were sequenced by a judicious combination of mass spectrometric peptide sequencing and automated Edman degradation. The C-2 fragments were ordered on the basis of methionine-containing peptides identified by gas chromatographic mass spectrometry, while C-1 and C-2 were arranged by analysis of an overlapping CNBr fragment.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	1
Volume Number	76
Language	English
Publisher	National Academy of Sciences
Publisher Date	1979-05-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bacteriorhodopsins Carotenoids Amino Acid Sequence Chromatography, Gel Chromatography, High Pressure Liquid Chymotrypsin Membrane Proteins Peptide Fragments Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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