The carbohydrate moiety of human platelet glycocalicin.
نویسندگان
چکیده
منابع مشابه
The carbohydrate moiety of bovine pancreatic deoxyribonuclease.
Preceding experiments by Price and his associates establish that bovine pancreatic deoxyribonuclease is a glycoprotein which contains glucosamine and mannose. In order to determine the mode of attachment of the carbohydrate to the enzyme molecule, chromatographically purified deoxyribonuclease has been digested with Pronase. Gel filtration of the digest yielded a fraction containing all of the ...
متن کاملPlatelet glycocalicin. Interaction with thrombin and role as thrombin receptor of the platelet surface.
Intact human platelets contain on their outer surface a glycoprotein, glycocalicin (M, = 150,000). which is released in soluble form following platelet homogenization while glycoprotein I, which has a similar electrophoretic mobility, remains bound to the plasma membrane (Okumura, T., and Jamieson, G. A. (1976)5. Bid. Chem. 251, 5944-5949). Purified glycocalicin has now been shown to be a compe...
متن کاملApparent dispensability of the carbohydrate moiety of human interferon for antiviral activity.
Human leukocyte and tritium-labeled fibroblast interferons, prepared by induction with Sendai virus and with double-stranded polyinosinic acid.polycytidylic acid respectively, have been studied in relation to the carbohydrate moieties attached to them. These interferons were partially purified by immunoabsorbance and by gel filtration. On treatment with glycosidases, about 80% of the 3H-labeled...
متن کاملImmunosuppression by human plasma alpha 1-acid glycoprotein: importance of the carbohydrate moiety.
Human plasma alpha 1-acid glycoprotein (orosomucoid) and derivatives of this protein produced by sequential enzymatic cleavage of the glycosidic residue (sialic acid, galactose, N-acetylglucosamine, mannose) were tested for the ability suppress a number of immune functions of mouse spleen cells in vitro at physiological concentrations. alpha 1-Acid glycoprotein and especially the agalacto/asial...
متن کاملFibrin Monomer Induces Binding of Endogenous Platelet von Willebrand Factor to the Glycocalicin Portion of Platelet Glycoprotein lB
This study demonstrates that when platelets are stimulated by thrombin in the presence of low concentrations of purified human fibrinogen (10 to 20 Lg/mL. final concentration) binding of released platelet von Willebrand factor (plt-vWF) to the platelet membrane is enhanced. This effect appears to be mediated by fibrin monomer produced by the action of thrombin on the fibrinogen in the incubatio...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1983
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)32413-x