Immunological Cross-Reactivity between Electric-Eel Acetylcholinesterase and Rat-Tail-Tendon Collagen
نویسندگان
چکیده
منابع مشابه
Nanomechanical mapping of hydrated rat tail tendon collagen I fibrils.
Collagen fibrils play an important role in the human body, providing tensile strength to connective tissues. These fibrils are characterized by a banding pattern with a D-period of 67 nm. The proposed origin of the D-period is the internal staggering of tropocollagen molecules within the fibril, leading to gap and overlap regions and a corresponding periodic density fluctuation. Using an atomic...
متن کاملChromatographic fractionation of acetic acid-solubilized rat tail tendon collagen.
It has been known since before 1870 (1) that collagen swells in dilute acetic acid, loses its fibrillar appearance, and eventually dissolves, in part, to yield a viscous solution. If the temperature of this solution is raised steadily, its viscosity decreases, at first slightly, then sharply, a phenomenon which occurs between 13” and 40”, depending on the type of collagen (2). Physical measurem...
متن کاملImmunological cross-reactivity between human tripeptidyl
Tripeptidyl peptidase II (TPP II) is a large intracellular exopeptidase with an active site of the subtilisin type. Affinitypurified hen antibodies against human erythrocyte TPP II cross-reacted with fibronectin in an immunoblot analysis. Furthermore, antibodies against human fibronectin cross-reacted with TPP II. Antibodies against a 65 kDa cell-binding fragment of fibronectin specifically rea...
متن کاملPurification, properties and immunological cross-reactivity
The bifunctional P protein (chorismate mutase : prephenate dehydratase) from Acinetobacter calcoaceticus has been purified. It was homogeneous in polyacrylamide gels and was more than 95% pure on the basis of the immunostaining of purified P protein with the antibodies raised against the P protein. The native enzyme is a homodimer ( M , = 91 000) composed of 45-kDa subunits. A twofold increase ...
متن کاملProteoglycan-collagen arrangements in developing rat tail tendon. An electron microscopical and biochemical investigation.
1. Developing tail tendons from rats (19-day foetal to 126 days post partum) were examined by electron microscopy after staining for proteoglycan with a cationic copper phthalocyanin dye. Cuprolinic Blue, in a "critical electrolyte concentration" method. Hydroxyproline was measured on papain digests of tendons, from which glycosaminoglycuronans were isolated, characterized and quantified. 2. Me...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1979
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1979.tb12867.x