Homology between rabbit uteroglobin and the rat seminal vesicle sperm-binding protein: Prediction of structural features of glutamine substrates for transglutaminase

S. Metafora, F. Facchiano, A. Facchiano, C. Esposito, G. Peluso, R. Porta

Research output: Contribution to journalArticlepeer-review

Abstract

A comparison of both amino acid composition and sequence of the rabbit uteroglobin (UG) subunit and the rat seminal vesicle sperm-binding protein (rSBP) by computer analysis indicates homology between the two polypeptide chains. These findings are supported by immunological studies showing the occurrence of similar antigenic determinants. In addition, our data indicate the glutamine-9 of the rat seminal vesicle sperm-binding protein and glutamine-40 of UG as the possible glutamine residues involved when the proteins act as transglutaminase (TGase) substrates. The latter results represent an interesting approach to determining the general structural features of the acyl donor site in the TGase-catalyzed reaction.

Original languageEnglish
Pages (from-to)353-359
Number of pages7
JournalJournal of Protein Chemistry
Volume6
Issue number4
DOIs
Publication statusPublished - Aug 1987

Keywords

  • protein homology
  • seminal vesicle
  • sperm-binding protein
  • transglutaminase
  • Uteroglobin

ASJC Scopus subject areas

  • Biochemistry

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