A new antigen was isolated from human tissue extracts. By immunofluorescence it was found only in granulocytic cells both in the cytoplasm and on the surface of these cells. It is an alpha-globulin having a molecular weight of approximately 47,000. It is unglycosylated and does not bind to various lectins. Due to its electrophoretic mobility and its cellular localization, it was named alpha-G (for granulocytes) globulin.
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http://dx.doi.org/10.1016/0165-2478(85)90035-5 | DOI Listing |
Prep Biochem Biotechnol
February 2015
a CSIR-Centre for Cellular and Molecular Biology, Hyderabad , India.
Protein recovery from gel electrophoresis plays a significant role in functional genomics and proteomics. To assist in this, a simple, cost-effective, and efficient apparatus for electroelution of proteins has been designed. The performance of the apparatus was demonstrated using the proteins bovine serum albumin (BSA), phosphorylase, ovalbumin, pepsin, and trypsinogen.
View Article and Find Full Text PDFA new antigen was isolated from human tissue extracts. By immunofluorescence it was found only in granulocytic cells both in the cytoplasm and on the surface of these cells. It is an alpha-globulin having a molecular weight of approximately 47,000.
View Article and Find Full Text PDFMacrophage migration inhibitory activity from Zajdela hepatoma ascites (AH-MIF) was characterized by ion exchange chromatography, gel filtration and isoelectric focusing. The data obtained indicate molecular heterogeneity according to net charge as revealed by chromatography on DEAE-Sephadex A-50. Furthermore, molecular sieve chromatography with Sephadex G-100 demonstrated the existence of subfractions with molecular weights of about 45,000, 20,000 and 10,000 - 15,000 respectively.
View Article and Find Full Text PDFBiochim Biophys Acta
February 1980
A crude extract of the proventriculus of the Japanese quail gave at least five bands of peptic activity at pH 2.2 on polyacrylamide gel electrophoresis. The main component, constituting about 40% of the total acid protease activity, was purified to homogeneity by hydroxyapatite and DEAE-Sepharose column chromatographies.
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