Journal:

Article Title: Dynamics of Bacterial Community Composition and Activity during a Mesocosm Diatom Bloom

doi:

Figure Lengend Snippet: DGGE profiles of the bacterial community composition over time in tanks 1 and 3. Separate gels (each with 30 to 46% denaturant gradients) were used for the two tanks. Each excised, cloned, and sequenced band is numbered on the left. The relationships of excised band sequences to other sequences in the GenBank database are indicated in the table under the gels.

Article Snippet: Electrophoresis was performed with a hot-bath denaturing gradient gel electrophoresis (DGGE) unit (CBS Scientific, Del Mar, Calif.) using 0.5× TAE running buffer (20 mM Tris, 10 mM acetate, 0.5 mM Na 2 -EDTA, pH 8.2) at 60°C for 5.5 h at 200 V. Gels were stained for 30 min in SYBR Green I nucleic acid stain (Molecular Probes), destained for 10 min in 0.5× TAE, and photographed with UV transillumination.

Techniques: Clone Assay

Journal: Scientific Reports

Article Title: Spiders’ digestive system as a source of trypsin inhibitors: functional activity of a member of atracotoxin structural family

doi: 10.1038/s41598-023-29576-y

Figure Lengend Snippet: Purification of Nephilingis cruentata MMD inhibitors. ( A ) Bovine trypsin inhibitory assay with the eluted fractions from the ionic-exchange batch separation and respective controls. (C1): control assay of bovine trypsin with 25 mM of ammonium bicarbonate at pH 8.5; (C2): control assay of bovine trypsin 25 mM of ammonium bicarbonate containing 1 M NaCl at pH 8.5; (C3): control assay of bovine trypsin with 25 mM of ammonium bicarbonate at pH 3.5; (1): Fraction eluted with 25 mM of ammonium bicarbonate at pH 8.5; (2): Fraction eluted with 25 mM of ammonium bicarbonate with 1 M NaCl at pH 8.5; (3): Fraction eluted with 25 mM of ammonium bicarbonate at pH 3.5. Inhibitory activity was measured using bovine trypsin 12 ng/µl as enzyme source and (0.1 mM) ZFRMCA as substrate (N = 3). ( B ) Chromatographic separation profile (UV at 214 nm) of fraction 2 (inhibitory active fraction against bovine trypsin), using a C18 column. Elution was performed by a linear gradient of 5% to 90% of solution B in 35 min. ( C ) SDS-PAGE in a 4–20% polyacrylamide gel of chromatographic peaks (P1-P6). Lane S molecular mass marker (97–14 kDa); lanes respectively: 1: P1; 2: P2; 3: P3; 4: P4; 5: P5; and 6: P6. The red arrow shows a single band detected by Coomassie blue G-250R. The approximate mass for the band on line 4 is 28.78 kDa calculated by gel relative migration.

Article Snippet: The samples eluted from chromatography on RP-HPLC (10 μg of protein) were loaded on 4–20% gradient SDS- PAGE gel kit Biocompare ( www.biocompare.com ) in reducing conditions.

Techniques: Purification, Control, Activity Assay, SDS Page, Marker, Migration