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Bovine lactoperoxidase and its recombinant: comparison of structure and some biochemical properties.

Abstract：

:Biochemical properties of bovine lactoperoxidase isolated from milk and recombinant bovine lactoperoxidase expressed by Chinese hamster ovary cells were compared. The natural and recombinant lactoperoxidases showed the same conformational features as determined by circular dichroism (CD) measurements. The alpha-helix, beta-structure, and unordered structure contents were found to be 17. 8, 54.2, and 28.0% for the natural lactoperoxidase and 18.6, 50.1, and 31.3% for the recombinant lactoperoxidase, respectively. The microenvironments of aromatic amino acid residues in both lactoperoxidases seemed to be the same, although the CD spectral band due to the Soret band differed slightly. A difference in the pH-dependent spectral changes of absorbance at 413 nm was observed. From a pepsin hydrolysate of lactoperoxidase, a heme-binding peptide was isolated by reverse-phase HPLC and its amino acid sequence was examined.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Watanabe S,Murata S,Kumura H,Nakamura S,Bollen A,Moguilevsky N,Shimazaki K

doi

10.1006/bbrc.2000.3217

subject

Has Abstract

pub_date

2000-08-11 00:00:00

pages

756-61

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006291X00932170

journal_volume

274

pub_type

杂志文章

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