Abstract
Profilin is a low molecular weight protein involved in the organization of the mammalian and protozoan cytoskeleton as well as in signal transduction. In this study, profilin is identified as an actin-binding protein in higher plants which is present in monocot and dicot angiosperms. Birch pollen profilin and actin can be copurified as a complex, and purified recombinant birch profilin can be used as an affinity matrix to obtain birch pollen actin. The binding of 125I-labeled recombinant birch pollen profilin to plant and animal actins can be blocked by profilin-specific antibodies that react with different epitopes of birch profilin. One of the blocking antibodies was raised against the 25 COOH-terminal amino acids indicating the importance of this region in the profilactin complex formation.
Highlights
Profilin was identifiedas an important birch pollen allergen (Valenta et al 1991a) which led to further investigationof the occurrence, properties, and functions of profilins in plants
Profilin binds topolyengineered immediately adjacent to the most distal poly(A) processing site.’. This 1.4-kilobaseNcoIIBamHI fragment was cloned into the corresponding replacement region of the expression vector pET15b (Novagene).Aac8 actin protein was overexpressedin E. coli DE3 (Novagene) in the presence of 100pgiml ampicillinas per the supplier’s instructions phosphoinositides which reversibly seems to regulate the in- with the exception that the cells were allowed to grow overnight after teraction of profilin with actin
RP2 and RP4, were raised against purified recombinant birch profilin that had been expressed in E. coli JM105/pKK2233 (Valenta et al, 1991b).One rabbit was immunized with the 25 COOH-terminal amino acid peptide of birch profilin conjugated to keyhole limpet hemocyanin using a conjugation kit (Pierce) to obtain antiserum RP3
Summary
Profilin was identifiedas an important birch pollen allergen (Valenta et al 1991a) which led to further investigationof the occurrence, properties, and functions of profilins in plants. RP2 and RP4, were raised against purified recombinant birch profilin that had been expressed in E. coli JM105/pKK2233 (Valenta et al, 1991b).One rabbit was immunized with the 25 COOH-terminal amino acid peptide of birch profilin conjugated to keyhole limpet hemocyanin using a conjugation kit (Pierce) to obtain antiserum RP3. Antibodies were tested for binding to the 25 COOH-terminal amino acids of birch profilin expressed in hgtll/E.
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