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Primary structure of human lymphotoxin derived from 1788 lymphoblastoid cell line.
Open accessAbstract
The amino acid sequence of human lymphotoxin derived from a 1788 lymphoblastoid cell line was determined. Peptide fragments obtained by trypsin, lysine-C peptidase, cyanogen bromide, and acetic acid cleavage of the intact protein were purified by reverse-phase high performance liquid chromatography and analyzed by amino acid composition and by automated Edman degradation. The protein is 171 amino acids long with a molecular weight of 18,664. It contains one asparagine-linked glycosylation site and lacks cysteine. The salient features of the amino acid sequence of lymphotoxin are described.
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Metadata
- Authors
- Aggarwal, B. B., Henzel, W. J., Moffat, B., Kohr, W. J., & Harkins, R. N.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1985-02
- Volume
- 260
- Issue
- 4
- Pages
- 2334-2344
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1593830931
- Cited by
- 170
- References
- 0
- FWCI
- 8.75
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Aggarwal, B. B., Henzel, W. J., Moffat, B., Kohr, W. J., & Harkins, R. N. (1985). Primary structure of human lymphotoxin derived from 1788 lymphoblastoid cell line. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)89559-x
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