Journal Article

Expression and characterization of Kunitz domain 3 and C-terminal of human tissue factor pathway inhibitor-2

Lina Zhu, Jiping Wang, Jingui Mu, Huijun Wang, Chenqi Zhang, Jue Wang, Xingang Liu, Xiaomin Yan, Linsen Dai and Duan Ma

in Acta Biochimica et Biophysica Sinica

Published on behalf of Institute of Biochemistry and Cell Biology, SIBS, CAS

Volume 41, issue 11, pages 948-954
Published in print November 2009 | ISSN: 1672-9145
Published online October 2009 | e-ISSN: 1745-7270 | DOI: http://dx.doi.org/10.1093/abbs/gmp089
Expression and characterization of Kunitz domain 3 and C-terminal of human tissue factor pathway inhibitor-2

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Human tissue factor pathway inhibitor-2 (hTFPI-2) is a serine protease inhibitor and its inhibitory activity is enhanced by heparin. The Kunitz domain 3 and C-terminal of hTFPI-2 (hTFPI-2/KD3C), which has the activity toward heparin calcium, have been successfully expressed in Pichia pastoris and purified by SP-Sepharose and heparin-Sepharose chromatography. The Fourier transformed infrared spectroscopy (FTIR), Raman spectroscopy, and circular dichroism (CD) experiment results implied that hTFPI-2/KD3C contained small contents of α-helix and β-strand, but large amounts of random coil and two kinds of disulfide bonds, gauche-gauche-gauche (ggg) and trans-gauche-trans (tgt). The interaction of hTFPI-2/KD3C with heparin calcium was investigated by CD. It was found that heparin calcium induced β-strands in hTFPI-2/KD3C to different extents depending on the ratio of hTFPI-2/KD3C and heparin calcium.

Keywords: Kunitz domain 3 and C-terminal of hTFPI-2; heparin; secondary structure; Pichia pastoris

Journal Article.  3528 words.  Illustrated.

Subjects: Biochemistry

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