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Putative rat sperm lipid-binding protein: isolation and partial characterization

J L Pryor1, W Xu, A Moore

  • 1Department of Cell Biology and Neuroanatomy, University of Minnesota, Minneapolis.

Molecular Reproduction and Development
|November 1, 1994
PubMed
Summary
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Researchers isolated a rat male reproductive protein (B109) and found it highly homologous to a bovine brain protein. Sequence analysis suggests amino acid substitutions, not post-translational modifications, explain differences between the rat and bovine proteins.

Area of Science:

  • Reproductive Biology
  • Molecular Biology
  • Protein Chemistry

Background:

  • A 22-24 kD protein is present in rat male reproductive tissues like the epididymis and testis.
  • This protein, designated B109, was targeted using a specific monoclonal antibody (mAb-B109).

Purpose of the Study:

  • To isolate and characterize the B109 protein from rat male reproductive tissues.
  • To determine the amino acid sequence and identify homologous proteins.

Main Methods:

  • Protein isolation via chromatofocusing, SDS-PAGE electroelution, and reverse-phase HPLC.
  • Internal amino acid sequencing through cyanogen bromide and chymotrypsin cleavage.
  • Homology search using the Protein Identification Resource (PIR) database.

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Main Results:

  • B109 protein (pI = 4.8) was isolated and found to be amino-terminal blocked.
  • Partial amino acid sequences were obtained from cleaved peptides.
  • B109 showed >80% homology to a 21-kD bovine brain cytosolic protein (pI = 7.4).
  • Sequence analysis indicated substitutions, not post-translational processing, account for pI differences.

Conclusions:

  • The rat B109 protein is highly homologous to a bovine brain protein, suggesting conserved function or evolutionary relationship.
  • Differences in isoelectric point (pI) are attributed to amino acid substitutions.
  • The function of B109 remains unknown, though the bovine homolog is linked to phospholipid transport.