The Journal of Experimental Medicine
StemCell Technologies
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JEM
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Cameron, P.
Right arrow Articles by Schmidt, J. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Cameron, P.
Right arrow Articles by Schmidt, J. A.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Journal of Experimental Medicine, Vol 162, 790-801, Copyright © 1985 by Rockefeller University Press

ARTICLES

Amino acid sequence analysis of human interleukin 1 (IL-1). Evidence for biochemically distinct forms of IL-1

P Cameron, G Limjuco, J Rodkey, C Bennett and JA Schmidt

The pI-6.8 species of normal human interleukin 1 (IL-1) has been isolated by ion-exchange and reverse-phase high-performance liquid chromatography. The isolated material had a molecular weight of 18,000, and had a specific bioactivity of 1.7 X 10(7) half-maximal U/mg in the murine thymocyte proliferation assay, values similar to those obtained for murine P388D1-derived IL-1 (12), and human IL-1 isolated by a previously published purification protocol (15). Amino-terminal sequence analysis revealed a single N-terminal, and resulted in the identification of 30 of the first 35 amino acid residues. Sequence of three CNBr cleavage fragments of purified IL-1 resulted in the identification of an additional 38 residues. All of the sequences agree exactly with those deduced from complementary DNA (cDNA) by Auron, et al. (18), demonstrating that this cloned cDNA, though considerably different from the cDNA reported for murine IL-1 (12), nevertheless codes for the pI-6.8 species of human IL-1. The evidence also shows that the precursor protein for human IL-1 is largely processed at the N- terminal end. Little or no processing occurs at the carboxy-terminal end. Sequence homology with interferon-inducing factor (26) suggests that the pI-6.8 species of human IL-1 is a member of a gene family. Although equally potent in the murine thymocyte proliferation assay, murine IL-1 and the pI-6.8 species of human IL-1 are structurally distinct. Further study will answer the interesting question as to the relationship of the other charged species of human IL-1 to these distinct IL-1 classes.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:



  Home | Help | Feedback | Subscriptions | Archive | Search
TABLE OF CONTENTS