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Functional properties of peptides derived from seminalplasmin: Binding to monospecific anti-seminalplasmin immunoglobulins G and calmodulin.

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Krauhs,  E.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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Preuss,  K. D.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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Scheit,  K. H.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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Citation

Krauhs, E., Preuss, K. D., & Scheit, K. H. (1990). Functional properties of peptides derived from seminalplasmin: Binding to monospecific anti-seminalplasmin immunoglobulins G and calmodulin. Biological Chemistry Hoppe-Seyler, 371(2), 111-116.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0013-0E5C-2
Abstract
Seminalplasmin was specifically hydrolysed employing the proteinases Lys-C and Glu-C. A set of peptides of seminalplasmin were obtained which were used to study their interaction with monospecific anti-seminalplasmin IgGs as well as calmodulin. Two peptides P4 (position 38-47) and P9 (position 4-32) strongly interacted with the polyclonal anti-seminalplasmin IgGs, indicating that a C-terminal (P4) as well as a N-terminal region of seminalplasmin represent major antigenic sites of the polypeptide. From the panel of peptides only peptide P9 was found to bind to calmodulin with high affinity. Thus, the structural requirements for the strong and specific interaction of calmodulin with seminalplasmin apparently reside in the N-terminal sequence 3-32 of the latter.