| Literature DB >> 7758455 |
R Gieselmann1, D J Kwiatkowski, P A Janmey, W Witke.
Abstract
The biochemical characteristics of a new human profilin isoform are described. We refer to this recently described isoform as profilin II (isoelectric point 5.9) in comparison to profilin I (pI 8.4). We expressed both isoforms in bacteria and compared their actin-binding properties, binding to poly(L-proline), affinities for phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2], and their effects on nucleotide exchange on actin. Profilin I and profilin II have similar affinities for PtdIns(4,5)P2 and poly(L-proline), and both accelerate nucleotide exchange on monomeric actin to the same extent. However, the affinity of profilin I for monomeric actin is about five times higher than the affinity of profilin II for actin. Potential structural differences of profilin I and profilin II that might explain the difference in actin binding are discussed.Entities:
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Year: 1995 PMID： 7758455 DOI： 10.1111/j.1432-1033.1995.tb20506.x
Source DB: PubMed Journal: Eur J Biochem ISSN： 0014-2956