Zobrazeno 1 - 7
of 7
pro vyhledávání: '"J. A. Ripellino"'
Publikováno v:
The Journal of biological chemistry. 269(4)
The beta-amyloid precursor protein (beta-APP) is a membrane spanning glycoprotein. The small beta-protein domain within the precursor is presumed to be the source of amyloid found in plaques characteristic of Alzheimer's disease. The amino terminus o
Publikováno v:
The Journal of biological chemistry. 267(20)
The Alzheimer's amyloid beta protein is derived from a family of membrane glycoproteins termed amyloid precursor proteins (APP). Here we show that APP exists as the core protein of a chondroitin sulfate (CS) proteoglycan, ranging in apparent molecula
Autor:
J. A. Ripellino, John S. Elam
Publikováno v:
Neurochemical Research. 5:351-360
Metabolic turnover of axonally transported glycoproteins has been examined in membranous and soluble subfractions of goldfish optic tectum following intraocular injection of [3H]fucose. Radioactivity in total transported glycoproteins reached a maxim
Publikováno v:
Annals of the New York Academy of Sciences. 481:46-54
Publikováno v:
Biochemical and Biophysical Research Communications. 145:1142-1148
After biosynthetic labeling of sulfated glycoproteins in rat and goldfish brain and PC12 pheochromocytoma cells with sodium [ 35 S]sulfate, it was observed that all of the bands reactive with the HNK-1 antibody on immunoblots of sodium dodecyl sulfat
Publikováno v:
The Journal of Cell Biology
The hyaluronic acid-binding region was prepared by trypsin digestion of chondroitin sulfate proteoglycan aggregate from the Swarm rat chondrosarcoma, and biotinylated in the presence of hyaluronic acid and link protein. After isolation by gel filtrat
Publikováno v:
The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society. 33(10)
The hyaluronic acid binding region was prepared by clostripain digestion of chondroitin sulfate proteoglycan isolated from the Swarm rat chondrosarcoma, and biotinylated in the presence of associated hyaluronic acid and link protein. After removal of