Abstract:
:Bovine milk alpha-lactalbumin (alpha-La) was mixed with soybean saponin, and the resulting mixture was hydrolyzed by trypsin. Saponin increased the tryptic-hydrolysis level of alpha-La only at relatively high phosphate buffer concentrations (> or = 0.05 M). T(1) experiments with acetylated soybean saponin demonstrated that there were some interactions between alpha-La and saponin not only at high concentrations of phosphate buffers but even at low concentrations as well. Circular dichroism spectra of alpha-La showed that the tertiary structure of alpha-La was changed through interactions with saponin only at high buffer concentrations. Furthermore, by analyzing the tryptic peptides from an alpha-La/saponin mixture, hydrolyzing rates at all or some of K5, R10, and K16 of alpha-La were accelerated by saponin interactions. The increase in the tryptic hydrolysis of alpha-La by saponin addition was considered due to modification of the tertiary structure of alpha-La by saponin.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Shimoyamada M,Okada Y,Watanabe K,Yamauchi Rdoi
10.1016/j.abb.2005.01.001subject
Has Abstractpub_date
2005-03-15 00:00:00pages
273-9issue
2eissn
0003-9861issn
1096-0384pii
S0003-9861(05)00002-0journal_volume
435pub_type
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