Loading…

Characterization of Monomeric and Homodimeric Forms of Osteoclastogenesis Inhibitory Factor

Osteoclastogenesis inhibitory factor (OCIF) is present naturally as two molecular forms, a monomer and a homodimer. The two forms of recombinant human OCIF (rOCIF) produced by Chinese hamster ovary (CHO) cells were purified to homogeneity. Determination of the C-terminal amino-acid sequences of the...

Full description

Saved in:
Bibliographic Details
Published in:Biochemical and biophysical research communications 1998-04, Vol.245 (2), p.382-387
Main Authors: Tomoyasu, Akihiro, Goto, Masaaki, Fujise, Nobuaki, Mochizuki, Shin-ichi, Yasuda, Hisataka, Morinaga, Tomonori, Tsuda, Eisuke, Higashio, Kanji
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Osteoclastogenesis inhibitory factor (OCIF) is present naturally as two molecular forms, a monomer and a homodimer. The two forms of recombinant human OCIF (rOCIF) produced by Chinese hamster ovary (CHO) cells were purified to homogeneity. Determination of the C-terminal amino-acid sequences of the two forms of rOCIF revealed that the monomeric rOCIF lacked several amino acids including Cys379, which is involved in the intermolecular disulfide bond, in its C-terminal region. The two forms of rOCIF were indistinguishable in stability, sialic acid content, and specific activity in inhibition of osteoclastogenesis. In contrast, the homodimeric rOCIF was stronger in heparin-binding ability than the monomeric rOCIF. The homodimeric rOCIF was significantly shorter in initial half-life and smaller in AUC value in rats than the monomeric rOCIF, but exerted more potent biological activity in reducing the calcium concentration in serum of rats than did the monomeric rOCIF.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1998.8443