Purification and partial characterization of alkaline phosphatase of matrix vesicles from fetal bovine epiphyseal cartilage. Purification by monoclonal antibody affinity chromatography.
Open Access
- 1 February 1985
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 260 (3) , 1826-1831
- https://doi.org/10.1016/s0021-9258(18)89667-3
Abstract
No abstract availableThis publication has 21 references indexed in Scilit:
- Solubility properties of alkaline phosphatase from matrix vesiclesBiochimica et Biophysica Acta (BBA) - General Subjects, 1983
- Production of a monoclonal antibody to human liver alkaline phosphataseClinica Chimica Acta; International Journal of Clinical Chemistry, 1982
- Ultrasensitive Stain for Proteins in Polyacrylamide Gels Shows Regional Variation in Cerebrospinal Fluid ProteinsScience, 1981
- Enzymatic characterization of the matrix vesicle alkaline phosphatase isolated from bovine fetal epiphyseal cartilageCalcified Tissue International, 1980
- Enzymatic characterization of the chondrocytic alkaline phosphatase isolated from bovine fetal epiphyseal cartilageBiochimica et Biophysica Acta (BBA) - Enzymology, 1979
- Electrolytes of isolated epiphyseal chondrocytes, matrix vesicles, and extracellular fluidCalcified Tissue International, 1977
- A simple and defined method to study calcification by isolated matrix vesicles effect of ATP and vesicle phosphataseBiochimica et Biophysica Acta (BBA) - General Subjects, 1977
- Intestinal alkaline phosphatase. Physical properties and quaternary structureBiochemistry, 1974
- Isolation and Characterization of Calcifying Matrix Vesicles from Epiphyseal CartilageProceedings of the National Academy of Sciences, 1970
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970