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The VIJEO.SCADA.V7.1 32. OMRON.CX‐ONE v4.1 33. OMRON NS Designer V6.2 34.Tropoelastin in elastin-predominant regions of the rat aorta is resistant to endo-beta-N-acetylglucosaminidase H.
A polyclonal antibody was raised against partially purified rat aortic tropoelastin. With this antibody tropoelastin was detected in rat aortas by immunoblotting and immunocytochemistry. The antibody also stained elastic fibers in the media of the aorta in a pattern similar to that with an anti-tropoelastin monoclonal antibody, which recognizes a region of tropoelastin immunologically related to microfibrillar elastic fiber-associated tropoelastin in human skin (alpha-tropomyosin regions A and B). In the absence of carbohydrate or glycoprotein-specific reagents, a panel of glycosidase enzymes was used to determine whether the antigenic determinants recognized by the anti-tropoelastin antibody were located in carbohydrate residues. Endo-beta-N-acetylglucosaminidase H (endo-beta-N-acetylglucosaminidase H) progressively removed tropoelastin along with blood group B glycolipids from elastin-predominant regions (EPs) of the aorta. After removal of approximately 30% of the carbohydrate residues by endo-beta-N-acetylglucosaminidase H, tropoelastin in these EPs was only partially digested to an apparent size of 35 kDa. Complete digestion occurred upon removal of 50% of the carbohydrate residues by endo-beta-N-acetylglucosaminid
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