Rat liver gap junction protein: Properties and partial sequence
Abstract
Gap junctions, strongly implicated as channels for direct cell-to-cell communication, have been isolated from rat liver in high yield and purity. These gap junction fractions contain few morphologically recognizable contaminants, but NaDodSO4/polyacrylamide gel electrophoresis reveals a number of polypeptides. With the exception of a nonjunctional component of Mr 38,000 and some poorly soluble material, including collagen, all the polypeptides have very similar or identical two-dimensional peptide maps and arise from proteolytic cleavage of the COOH-terminus or aggregation of a Mr 28,000 protein. We report the sequence of the NH2-terminal 52 amino acids of this protein. The polypeptide (Mr approximate to 10,000) characteristic of trypsin-treated gap junction preparations is shown to be two distinct polypeptides, both derived from the Mr 28,000 protein.
Additional Information
Copyright © 1981 by the National Academy of Sciences. Communicated by Norman Davidson, August 27, 1981. We thank Dr. Larry Takemoto for his guidance in the use of peptide mapping and Drs. David Meyer and Barbara Yancey for many fruitful discussions. The research was supported by Research Grant GM 06965 and Biomedical Research Support Program RR 07003 from the National Institutes of Health as well as a Ross Foundation Fellowship awarded to B.J.N. The publication costs ofthis article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact.Files
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Additional details
- Eprint ID
- 1333
- Resolver ID
- CaltechAUTHORS:NICpnas81
- Created
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2006-01-11Created from EPrint's datestamp field
- Updated
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2020-03-03Created from EPrint's last_modified field