Cell-free translation of messenger RNA for chondroitin sulphate proteoglycan core protein in rat cartilage.

نویسندگان

  • B M Vertel
  • W B Upholt
  • A Dorfman
چکیده

Total RNA was extracted from the cartilage tissues rat Swarm chondrosarcoma, neonatal-rat breastplate and embryonic-chicken sterna and translated in wheat-germ cell-free reactions. The core protein of the chondroitin sulphate proteoglycan subunit was identified among translation products of rat mRNA by its apparent Mr of 330 000 and by its immunoprecipitation with specific antisera prepared against rat or chicken proteoglycan antigens. The apparent Mr of the rat proteoglycan core protein is 8000-10000 less than that of the equivalent chicken cartilage core-protein product.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

hyaluronate, in chondrocytes

Cartilage proteoglycans are complex macromolecules in which many glycosaminoglycan chains are attached to a protein core. Chondrocytes isolated from the Swarm rat chondrosarcoma have been shown to produce cartilage-type proteoglycans in culture. The proteoglycans are secreted from the cells as monomers, but form aggregates in the culture medium by binding to hyaluronate and a specific link prot...

متن کامل

Cell adhesion and proteoglycans. I. The effect of exogenous proteoglycans on the attachment of chick embryo fibroblasts to tissue culture plastic and collagen.

Proteoglycan was isolated from cartilage and freed from contaminating glycoproteins and hyaluronic acid. The macromolecule consists of a protein core covalently linked to a number of glycosaminoglycan side chains, namely chondroitin sulphate and keratan sulphate. This proteoglycan retards the attachment of a variety of cell types to tissue culture plastic and to collagen. Glycosaminoglycans alo...

متن کامل

The metabolic fate of chondroitin (35S)sulphate proteoglycan in the rat.

Revell & Muir (1972) have studied the metabolism of 35S-labelled proteoglycan from porcine cartilage after injection into guinea pigs. They concluded that the polymeric material excreted in the urine was the result of proteolytic degradation of the injected proteoglycan to single chains of chondroitin sulphate. These results are particularly interesting with respect to the site(s) and mechanism...

متن کامل

The detection of substructures within proteoglycan molecules. Electron-microscopic immuno-localization with the use of Protein A-gold.

Proteoglycan monomers from pig laryngeal cartilage were examined by electron microscopy with benzyldimethylalkylammonium chloride as the spreading agent. The proteoglycans appeared as extended molecules with a beaded structure, representing the chondroitin sulphate chains collapsed around the protein core. Often a fine filamentous tail was present at one end. Substructures within proteoglycan m...

متن کامل

Immunochemical analysis of cartilage proteoglycans

Antibodies directed against whole bovine nasal-cartilage proteoglycan and against the hyaluronic acid-binding region and chondroitin sulphate peptides from the same molecule were used in immunodiffusion and immunoelectromigration experiments. Proteoglycans from bovine nasal and tracheal cartilage showed immunological identity, with all three antisera. Proteoglycans from pig hip articular cartil...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • The Biochemical journal

دوره 217 1  شماره 

صفحات  -

تاریخ انتشار 1984