Zobrazeno 1 - 10
of 150
pro vyhledávání: '"Lactose binding"'
Autor:
Mouad Toumi, Mohammed Elamine Smaali, Salvatore Calogero Gaglio, Mohammed Esseddik Toumi, Imene Torche, Angela Lauriola, Malik Ayadi, Redouane Rebai, Fethi Farouk Kebaili, Youcef Necib, Massimiliano Perduca
Publikováno v:
International Journal of Medicinal Mushrooms. 23:45-57
Mushroom lectins have important biological and biomedical applications. Most lectins purified from these organisms exhibit high toxicity in animal cells and toward microbial agents. They are able to induce cell growth inhibition and metabolism by the
Autor:
Sanjay Naik, Sanjit Kumar
Publikováno v:
ACS Omega, Vol 5, Iss 27, Pp 16430-16439 (2020)
A novel Entadin lectin was isolated, purified, and characterized from the seeds of Entada rheedii by ammonium sulfate precipitation, followed by lactose affinity chromatography. On sodium dodecyl sulfate polyacrylamide gel electrophoresis, the purifi
Autor:
Ahmmed, M. K., Bhowmik, S., Giteru, S. G., Zilani, M. N. H., Adadi, P., Islam, S. S., Kanwugu, O. N., Haq, M., Ahmmed, F., Ng, C. C. W., Chan, Y. S., Asadujjaman, M., Chan, G. H. H., Naude, R., Bekhit, A. E. -D. A., Ng, T. B., Wong, J. H.
Publikováno v:
Marine Drugs
Lectins are a unique group of nonimmune carbohydrate-binding proteins or glycopro-teins that exhibit specific and reversible carbohydrate-binding activity in a non-catalytic manner. Lectins have diverse sources and are classified according to their o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______917::483f4b3f5a5cf618886807ab6460ce80
https://hdl.handle.net/10995/117961
https://hdl.handle.net/10995/117961
Publikováno v:
Molecular biotechnology. 64(3)
Lectins are glycoproteins and known for their peculiar carbohydrate-binding activity and their insect-pest-resistant properties. Earlier we have published our research finding on novel gene encoding Bowman–Birk type protease inhibitor with insectic
Autor:
Yifa Zhou, Xuejiao Xu, Kevin H. Mayo, Guihua Tai, Qiuyu Han, Yuan Yao, Wenlu Zhang, Gabriela Jaramillo Ayala, Xumin Li, Jiyong Su, Yunlong Si
Publikováno v:
Biochimica et biophysica acta. General subjects. 1865(1)
Background The structure of human galectin-16 (Gal-16) has yet to be solved, and its function has remained elusive. Methods X-ray crystallography was used to determine the atomic structures of Gal-16 and two of its mutants. The Gal-16 oligomer state
Autor:
Bruna Coelho de Andrade, Luis Fernando Saraiva Macedo Timmers, Gaby Renard, Giandra Volpato, Claucia Fernanda Volken de Souza
Publikováno v:
Biotechnology Progress. 36
Hydrolysis efficiency of β-galactosidases is affected due to a strong inhibition by galactose, hampering the complete lactose hydrolysis. One alternative to reduce this inhibition is to perform mutations in the enzyme's active site. The aim of this
Autor:
Kátia Flávia Fernandes, P.M. Fernandes, Cassio Nazareno Silva da Silva, Ivan T.N. Campos, Karla A. Batista
Publikováno v:
Separation and Purification Technology. 185:54-60
The global prevalence of individuals with lactose intolerance and galactosemia has created a new market for commercially available lactose-free food products. In this scenario, the use of systems containing lactose-binding molecules for lactose remov
Autor:
Yunlong Si, Jiyong Su, Tong Yang, Kevin H. Mayo, Yuying Li, Yifa Zhou, Gabriela Jaramillo Ayala, Xumin Li, Guihua Tai
Publikováno v:
The FEBS journalReferences. 288(3)
The expression of prototype galectin-14 (Gal-14) in human placenta is higher than any other galectin, suggesting that it may play a role in fetal development and regulation of immune tolerance during pregnancy. Here, we solved the crystal structure o
Publikováno v:
Journal of Fish Biology. 89:1692-1703
This study represents the first report of a C-type lectin (ctl) in yellow catfish Tachysurus fulvidraco. The complete sequence of ctl complementary (c)DNA consisted of 685 nucleotides. The open reading frame potentially encoded a protein of 177 amino
Publikováno v:
Biotechnology and Bioengineering. 113:1666-1675
α1,3-Fucosyltransferase (α1,3-FucT) is essential for the biosynthesis of biologically active α1,3-fucosyloligosacchairdes (3-FOs) from human milk oligosaccharides (HMO), particularly 3-fucosyllactose (3-FL) trisaccharide. α1,3-FucT from Helicobac