Characterization of bovine heparin-binding neurotrophic factor (HBNF): Assignment of disulfide bonds

L. Fabri, E. C. Nice, L. D. Ward, H. Maruta, A. W. Burgess, R. J. Simpson

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Abstract

The topology of the disulfides in native heparin-binding neurotrophic factor (HBNF) isolated from bovine brain was studied by proteolytic digestion using trypsin, Asp-N endoproteinase and chymotrypsin and peptide mapping. Disulfide-linked peptides were identified by automated Edman degradation. It has been shown that there are disulfide bonds between Cys15-Cys44, Cys23-Cys53, Cys30-Cys57, Cys67-Cys99 and Cys77-Cys109.

Original languageEnglish
Pages (from-to)1-9
Number of pages9
JournalBiochemistry International
Volume28
Issue number1
Publication statusPublished - 1 Jan 1992
Externally publishedYes

Cite this

Fabri, L., Nice, E. C., Ward, L. D., Maruta, H., Burgess, A. W., & Simpson, R. J. (1992). Characterization of bovine heparin-binding neurotrophic factor (HBNF): Assignment of disulfide bonds. Biochemistry International, 28(1), 1-9.