Characterization of the protein and glycan moieties in different forms of bovine lactoferrin

Bioscience, Biotechnology, and Biochemistry
X Y YeS Yoshida

Abstract

The BrCN cleavage of lactoferrin-a or -b (LF-a or LF-b) led to the observation of four fragments by SDS-PAGE, whose molecular masses were 77, 58, 52, and 30 kDas, or 74, 54, 47, and 30 kDas, respectively. N-Terminal amino acid sequence analyses show that the sequences of 58, 52, and 30 kDa fragments (residues 64-471, 130-471, and 472-689) of LF-a coincide with those of the 54, 47, and 30 kDa fragments of LF-b. respectively. All these fragments, which were positive by PAS staining, were not stained after being treated with glycopeptidase F. This treatment changed the 58 and 52 kDa fragments of LF-a to the 54 and 47 kDa fragments, respectively, whose molecular masses were the same as those of the treated fragments of LF-b. The 58 and 52 kDa fragments of LF-a bound to the lectin, Ricinus communis agglutinin, while the 54 and 47 kDa fragments of LF-b hardly bound to it.

Citations

Jan 30, 2004·Regulatory Toxicology and Pharmacology : RTP·Steve TaylorMary Murphy
Feb 16, 2012·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·Agostina PietrantoniFabiana Superti
Jun 7, 2016·Journal of the American Chemical Society·Paweł PomastowskiBogusław Buszewski
Oct 26, 2000·Journal of Dairy Science·S YoshidaN Fukunaga
Mar 23, 2002·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·Paola RossiGiovanni Antonini
May 29, 2020·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·Kristina Zlatina, Sebastian P Galuska
Mar 23, 2021·Critical Reviews in Food Science and Nutrition·Yun-Shan WeiHong Wu

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