Journal: PLoS ONE

Article Title: Transcriptional Analyses of Natural Leaf Senescence in Maize

doi: 10.1371/journal.pone.0115617

Figure Lengend Snippet: Genes show high similarity to well-known SAGs in the SDEG dataset.

Article Snippet: GRMZM2G051943 , AT2G43570 , CHITINASE (CHI) , The senescence-enhanced genes , .

Techniques: Over Expression, Control, Starch, Mutagenesis

Journal: International Journal of Molecular Sciences

Article Title: Roles of Fatty Acids in Microglial Polarization: Evidence from In Vitro and In Vivo Studies on Neurodegenerative Diseases

doi: 10.3390/ijms23137300

Figure Lengend Snippet: Microglial phenotypes and their characteristics.

Article Snippet: Primary microglial cells were pretreated with DHA or EPA and stimulated with LPS, which resulted in the downregulation of NO, TNF-α, IL-6, and M1-specific markers, such as CCL5, CD14, CCL2, IL-23a, CCL4, IL-1α, and iNOS, and the upregulation of myelin phagocytosis and M2-specific markers (CCL22, CCL17, Arg1, IL-5, chitinase (Chi) 311, Gata3, CD206, CCL11, CCR2, transforming growth factor (TGF) β, and CCL1) ( ).

Techniques: Encapsulation

Journal: Microbial Cell Factories

Article Title: Molecular cloning, expression and biochemical characterisation of a cold-adapted novel recombinant chitinase from Glaciozyma antarctica PI12

doi: 10.1186/1475-2859-10-94

Figure Lengend Snippet: Domain organisation of family 18 chitinases; G. antarctica PI12 (CHI II), Bacillus cereus (chi 36) , Chaetomium cupreum (chi 58) , Saccharomyces cerevisiae (CTSI) , Lacanobia oleracea (Chitinase) and Bacillus circulans WL-12 (ChiD) .

Article Snippet: The recombinant chitinase CHI II protein (encoding CHI II mature protein) had an apparent molecular mass of about 39 kDa, less than the theoretically calculated molecular mass of 40.86 kDa.

Techniques:

Journal: Microbial Cell Factories

Article Title: Molecular cloning, expression and biochemical characterisation of a cold-adapted novel recombinant chitinase from Glaciozyma antarctica PI12

doi: 10.1186/1475-2859-10-94

Figure Lengend Snippet: Multiple sequence alignment of the core region of the catalytic domains between CHI II and some eukaryotic chitinases . Highly conserved regions, SxGG and DxxDxDxE, are boxed. Residues responsible for the catalytic activity are indicated with asterisks. Sequence fragments displaying the typical motifs with the G. antarctica PI12 catalytic domain include Amanita muscaria, Laccaria bicolor, Coprinellus congregatus, Puccinia triticina and Taiwanofungus camphorates .

Article Snippet: The recombinant chitinase CHI II protein (encoding CHI II mature protein) had an apparent molecular mass of about 39 kDa, less than the theoretically calculated molecular mass of 40.86 kDa.

Techniques: Sequencing, Activity Assay

Journal: Microbial Cell Factories

Article Title: Molecular cloning, expression and biochemical characterisation of a cold-adapted novel recombinant chitinase from Glaciozyma antarctica PI12

doi: 10.1186/1475-2859-10-94

Figure Lengend Snippet: Phylogenetic tree showing the relationship between CHI II from G. antarctica PI12 and other chitinases . The chitinase gene of S. griseus was used as an out-group to root the tree. Confidence values were assessed from 1,000 bootstrap replicates of the original sequence data.

Article Snippet: The recombinant chitinase CHI II protein (encoding CHI II mature protein) had an apparent molecular mass of about 39 kDa, less than the theoretically calculated molecular mass of 40.86 kDa.

Techniques: Sequencing

Journal: Microbial Cell Factories

Article Title: Molecular cloning, expression and biochemical characterisation of a cold-adapted novel recombinant chitinase from Glaciozyma antarctica PI12

doi: 10.1186/1475-2859-10-94

Figure Lengend Snippet: Purification of recombinant chitinase (CHI II) . Approximately 20 μl of sample was loaded into each well. M: protein molecular mass marker; Lane 1: crude concentrated enzyme; Lane 2 & 3: unbound fraction; Lane 3 & 4: elution fraction.

Article Snippet: The recombinant chitinase CHI II protein (encoding CHI II mature protein) had an apparent molecular mass of about 39 kDa, less than the theoretically calculated molecular mass of 40.86 kDa.

Techniques: Purification, Recombinant, Marker

Journal: Microbial Cell Factories

Article Title: Molecular cloning, expression and biochemical characterisation of a cold-adapted novel recombinant chitinase from Glaciozyma antarctica PI12

doi: 10.1186/1475-2859-10-94

Figure Lengend Snippet: Effect of pH (a) and temperature (b) on chitinase activity and stability . The highest chitinase activity was set to 100%.

Article Snippet: The recombinant chitinase CHI II protein (encoding CHI II mature protein) had an apparent molecular mass of about 39 kDa, less than the theoretically calculated molecular mass of 40.86 kDa.

Techniques: Activity Assay

Journal: Microbial Cell Factories

Article Title: Molecular cloning, expression and biochemical characterisation of a cold-adapted novel recombinant chitinase from Glaciozyma antarctica PI12

doi: 10.1186/1475-2859-10-94

Figure Lengend Snippet: Effect of metal ions and reagents on the recombinant CHI II chitinase activity . No addition (with no metals added to the enzyme solutions) was used for 100% relative activity.

Article Snippet: The recombinant chitinase CHI II protein (encoding CHI II mature protein) had an apparent molecular mass of about 39 kDa, less than the theoretically calculated molecular mass of 40.86 kDa.

Techniques: Recombinant, Activity Assay