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

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0013-0E5C-2 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-2FFD-3
Genre: Journal Article

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 Creators:
Krauhs, E.1, Author              
Preuss, K. D.1, Author              
Scheit, K. H.1, Author              
Affiliations:
1Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society, ou_578628              

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 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.

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Language(s): eng - English
 Dates: 1990-02
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: eDoc: 285674
ISI: A1990CR87100002
 Degree: -

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Title: Biological Chemistry Hoppe-Seyler
Source Genre: Journal
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Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 371 (2) Sequence Number: - Start / End Page: 111 - 116 Identifier: ISSN: 0177-3593