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Characterization by cDNA cloning of the mRNA for seminalplasmin, the major basic protein of bull semen.

MPS-Authors

Wagner,  S.
Max Planck Society;

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Freudenstein,  J.
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

Wagner, S., Freudenstein, J., & Scheit, K. H. (1990). Characterization by cDNA cloning of the mRNA for seminalplasmin, the major basic protein of bull semen. DNA and Cell Biology, 9(6), 437-442. doi:10.1089/dna.1990.9.437.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0013-0DA0-E
Abstract
A cDNA library derived from poly(A)+RNA of bull seminal vesicle tissue was screened with synthetic DNA probes specific for seminalplasmin (SAP), the major basic protein of bull semen. From a number of positive clones, pBSV12, containing a 577-bp insert, was identified and sequenced. The derived amino acid sequence comprises the known amino acid sequence of SAP with an amino terminal representing a putative signal sequence; at the carboxyl terminus the sequence contains an additional lysine residue. Present experimental data do not distinguish between two potential SAP precursor molecules, each starting with a methionine residue and differing by 10 amino acid residues in the leader peptide. Comparative Northern analysis reveals a SAP-specific mRNA of 700 bp, which lacks RNA from bovine testis as well as from seminal vesicle tissue of a bull calf; hence, expression of the SAP gene appears to be under androgen and/or developmental control. Southern analysis indicates that one gene appears to specify SAP. SAP-like DNA sequences were detected in ovine and porcine genomic DNA.