Methods for analysis of urinary glycosaminoglycans.

Methods for the analysis of urinary GAGs that can be used for or are applicable to routine assays are described. The most popular method for isolation of GAGs from a urine sample is CPC precipitation, in spite of the fact that it is time-consuming. To identify the different types of GAGs excreted, separation by one-dimensional cellulose acetate electrophoresis followed by staining with alcian blue or toluidine blue may suffice for routine purposes.

Isolation of dermatan sulfate with high heparin cofactor II-mediated thrombin-inhibitory activity from porcine spleen.

We prepared dermatan sulfate specimens from various porcine tissues, and compared their heparin cofactor II-mediated thrombin-inhibitory activities and chemical natures, including disaccharide composition. Electrophoresis of the specimens on cellulose acetate membrane indicated that spleen dermatan sulfate was the most acidic of the dermatan sulfates prepared from the various porcine tissues. Analysis of the disaccharide units of the dermatan sulfate specimens by high-performance liquid chromatography revealed that spleen dermatan sulfate was rich in 4,6-di-O-sulfated N-acetylgalactosamine residues as compared with those of the other tissues.

Isolation and characterization of fibronectin-binding proteoglycan carrying both heparan sulfate and dermatan sulfate chains from human placenta.

A proteoglycan was isolated from the human placenta by procedures including affinity chromatography with fibronectin immobilized on agarose. The glycosaminoglycan chains were found to be composed of heparan sulfate (86%) and dermatan sulfate (14%). The average molecular weights were estimated to be 1.

Isolation and characterization of a mucin-type glycoprotein from the lung lavage of a patient with alveolar proteinosis.

A high molecular weight glycoprotein was isolated from the lavage fluid of a patient with alveolar proteinosis by gel chromatography with Sepharose CL-4B. The glycoprotein gave a single band stainable with alcian blue and with periodate-Schiff reagent on the cellulose acetate membrane electrophoresis. The glycoprotein did not penetrate 3.

Inhibitory activities for thrombin and factor Xa of whale heparin: comparative studies on two preparations from different species.

Whale intestinal heparin preparations from Balaenoptera physalus L. (Bp) and Balaenoptera borealis L. (Bb) were fractionated by affinity chromatography on a column of antithrombin III (AT)-Sepharose 4B.