SDS-PAGE and Western blotting analysis of rBLfA (a) and rBLfN (b) deglycosylation. M Protein Marker (kDa, TIANGEN, Beijing); M′ Prestained protein marker (kDa, TIANGEN, Beijing); (a) 1 and 1′ rBLfA treated with Endo H; 2 and 2′ untreated rBLfA; 3 and 3′ deglycosylation reaction buffer; (b) 1 and 1′ rBLfN treated with Endo H; 2 and 2′ untreated rBLfN; 3 and 3′ negative control, double distilled water treated with Endo H
After deglycosylation (Fig. 3), the apparent molecular
weight of rBLfA and rBLfN was decreased from 43.0 and 41.5 kDa
to 42.0 and 40.5 kDa which were close to the calculated
molecular weight of His-tagged-peptides rBLfA (41.972 kDa) and
rBLfN (40.666 kDa).
Viewing this image requires a subscription. If you are a subscriber, please log in.
This image is from the article titled "Contribution of bovine lactoferrin inter-lobe region to iron binding stability and antimicrobial activity against Staphylococcus aureus
(from BioMetals), which is copyrighted by Springer Science+Business Media, LLC. For more information on the
copyright for this image, please refer to the full image caption and to the
The image is being made available for non-commercial purposes for subscribers to SpringerImages. For more information on what you are allowed to do with this image, please see our copyright policy.
To request permissions to use any copyrighted material, please visit the source document.
Report a copyright concern regarding this image.
Log in or register to save your favorite images and download them as high-quality PowerPoint or PDF files.
Log in or register to save your search criteria.
© Springer, part of Springer Science+Business Media.
Remote Address: 126.96.36.199 Server: 18