Reference

Microvascular heparinlike species with anticoagulant activity

Microvascular heparinlike species with anticoagulant activity. Marcum, James A.; Fritze, Linda; Galli, Stephen J.; Karp, George; Rosenberg, Robert D. (Dep. Med., Beth Israel Hosp., Boston, MA 02139, USA). Am. J. Physiol., 245(5, Pt. 1), H725-H733 (English) 1983. CODEN: AJPHAP. ISSN: 0002-9513. DOCUMENT TYPE: Journal CA Section: 13 (Mammalian Biochemistry) Calf-microvasculature was isolated from retina and cerebral gray matter. These prepns. contained 0.048-0.060 units of heparinlike anticoagulant activity/g wet tissue. The retinal microvascular material contained no detectable mast cells. The anticoagulant potency of this product was assocd. solely with endothelial cells. This property appears to be due to a heparinlike proteoglycan, since mol. species with biol. activity are pptd. with 10% (wt./vol. There are some commonly used reagents like 9005-49-6 in this article.) TCA and are destroyed by incubation with Flavobacterium heparinase. Furthermore, the above component functions in a manner virtually identical to heparin, since ~60% of these species with anticoagulant activity bind to antithrombin-ConA-Sepharose 4B, and only 15% of their biol. potency is expressed in the presence of antithrombin modified near the mucopolysaccharide-binding domain. The cerebral microvascular tissue contained a trace subpopulation of mast cells (~0.3%). The anticoagulant activity of this prepn. is probably assocd. with both endothelial cells and mast cells. .

Biochemical and immunochemical comparison of fibronectin and polynectin from porcine plasma

Biochemical and immunochemical comparison of fibronectin and polynectin from porcine plasma. Isemura, Mamoru; Hsu, Cheng Chin; Yamaguchi, Yu; Munakata, Hiroshi; Yosizawa, Zensaku; Nagai, Hiromi; Motomiya, Masakichi; Kan, Mikio; Yamane, Isao (Sch. Med.In this study， 9005-49-6 and 74-79-3 are also used., Tohoku Univ., Sendai 980, Japan). J. Biol. Chem., 259(2), 915-21 (English) 1984. CODEN: JBCHA3. ISSN: 0021-9258. DOCUMENT TYPE: Journal CA Section: 13 (Mammalian Biochemistry) Section cross-reference(s): 6 Polynectin, a glycoprotein of porcine blood plasma (also known as glycine-rich gelatin-binding protein), is similar to fibronectin with respect to binding characteristics to affinity gels. However, no immunopptn. reaction was obsd. either between polynectin and anti-fibronectin antiserum, or between fibronectin and antipolynectin antiserum. No cross-reaction was found between fibronectin and polynectin by ELISA. Immunohistochem. studies revealed the presence in abundance of polynectin in intestinal and gastric glands. The pattern of distribution of polynectin was entirely different from that of fibronectin. Polynectin, in contrast to fibronectin, exhibited no cell attachment-promoting effects on BHK-21, a baby hamster kidney cell line, and a cell line of human embryonic lung fibroblasts. In addn., changes in binding characteristics to affinity gels after redn. and alkylation differed between polynectin and fibronectin. Although both proteins appear to have similar carbohydrate chains, in view of the similar reactivities with lectins, polynectin is, apparently, entirely different from fibronectin. .