Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
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Construction and functional characterization of truncated versions of recombinant keratanase II from Bacillus circulans, H. Wang, W. He, P. Jiang, Y. Yu, L. Lin, X. Sun, M. Koffas, F. Zhang, Robert J. Linhardt, Glycoconjugate Journal, 34, 643–649, 2017.
There is a need for degradative enzymes in the study of glycosaminoglycans. Many of these enzymes are currently available either in their natural or recombinant forms. Unfortunately, progress in structure-activity studies of keratan sulfate (KS) have been impeded by the lack of a commercially available endo-β-N-acetylglucosaminidase, keratantase II. The current study uses a recently published sequence of a highly thermostable keratanase II identified in Bacillus circulans to clone and express a series of truncation mutants in Escherichia coli BL21. The resulting truncated forms of keratanase II exhibit activity and excellent storage and thermal stability making these useful tools for glycobiology research.;
Glycoconjugate Journal, 34, 643–649; Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
The Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; Glycoconjugate Journal; https://harc.rpi.edu/;