A thermostable alkaline protease was isolated from the Aspergillus niger Z1 strain in a liquid Czapek Dox medium, containing casein (1% w/v) as the sole nitrogen source. Enzyme extract was subjected to electrophoresis in SDS-polyacrylamide gel. Two protein bands were seen on polyacrylamide gel. Active enzyme was visualized in a zymogram and protease activity exhibited a molecular mass of 68 kDa...

Cultured rat Schwann cells are stimulated to divide by a protein growth factor, present in extracts of bovine brain and pituitary, which we have named glial growth factor (GGF). Two lines of evidence indicate that GGF activity in both brain and pituitary resides in a protein of Mr = 31,000. (1) Four independently isolated monoclonal antibodies that immunoprecipitate the activity react with an a...

A two-dimensional microfluidic system is presented for intact protein separations combining isoelectric focusing (IEF) and sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis (PAGE) employing in situ photopolymerized polyacrylamide (PAAm) gels. The PAAm gels are used for multiple functions. In addition to serving as a highly-resolving separation medium for gel electrophoresis, discr...

Sodium dodecyl sulphate polyacrylamide gel electrophoresis This procedure separates poplypeptides according to their size; as it is most commonly used proteins are resolved as a consequence of differences in their rates of migration. SDS/PAGE systems use buffers that contain a detergent, sodium dodecyl sulphate (SDS), which denatures proteins. In a solution of SDS most multi-subunit proteins ar...

An acid phosphatase has been isolated and purified from an extract of a germinating black gram seedling. The method was accomplished by gel filtration of a germinating black gram seedling crude extract on sephadex G-75 followed by ion exchange chromatography on DEAE cellulose. The acid phosphatase gave a single band on SDS-polyacrylamide slab gel electrophoresis. The molecular weight of the aci...

Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) is a universally used method for determining approximate molecular weight (MW) in protein research. Migration of protein that does not correlate with formula MW, termed "gel shifting" appears to be common for histidine-rich proteins but not yet studied in detail. We investigated "gel shifting" in Ni2+-binding histidine-rich H...