| Literature DB >> 8607858 |
T Komada1, R Araki, K Nakatani, I Yada, M Naka, T Tanaka.
Abstract
We isolated a new chemotactic protein from bovine lung, and its partial protein sequence analysis indicated that this protein was identical with S100L, one member of the Ca2+-binding S100 protein family. The chemotactic activity of S100L on guinea pig eosinophils is observed at 0.1nM protein concentration, and the effects appear mediated by a novel specific surface receptor. We characterized the receptor for S100L on guinea pig eosinophils. Scatchard analyses of the data that [125I]S100L bound to S100L receptor indicate the presence of two receptor populations on eosinophils with a Kd value of 3.3 x 10(-11)M and 1.1 x 10(-9)M. Thus, S100L protein has the most potent chemotactic activity on guinea pig eosinophils of all the chemotactic proteins.Entities:
Mesh:
Substances:
Year: 1996 PMID: 8607858 DOI: 10.1006/bbrc.1996.0496
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575