Purification of Human Erythrocyte Transglutaminase by Immunoaffinity Chromatography
- 1 December 1986
- journal article
- research article
- Published by Informa UK Limited in Preparative Biochemistry
- Vol. 16 (4), 321-335
- https://doi.org/10.1080/00327488608068752
Abstract
Human erythrocyte transglutaminase was purified using a reusable immunoaffinity column prepared from a monoclonal antibody described previously (Birckbichler et al., Hybridoma, 4, 179–186, 1985). The purified TGase was catalytically active and exhibited a single band of apparent Mr = 85, 000 on SDS-PAGE and Western blotting. The amino acid composition of the enzyme was determined. The amino terminus was blocked, and the carboxy-terminal residue appeared to be isoleucine.Keywords
This publication has 19 references indexed in Scilit:
- A Monoclonal Antibody to Cellular TransglutaminaseHybridoma, 1985
- Enhanced transglutaminase activity in transformed human lung fibroblast cells after exposure to sodium butyrateBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1983
- Increase in proliferative markers after inhibition of transglutaminase.Proceedings of the National Academy of Sciences of the United States of America, 1981
- TransglutaminasesAnnual Review of Biochemistry, 1980
- Presence in human epidermal cells of a soluble protein precursor of the cross-linked envelope: Activation of the cross-linking by calcium ionsCell, 1979
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- CELLULAR TRANSGLUTAMINASE, GROWTH, AND TRANSFORMATIONAnnals of the New York Academy of Sciences, 1978
- Human erythrocyte transglutaminase. Purification and propertiesBiochimica et Biophysica Acta (BBA) - Enzymology, 1978
- A filter paper assay for transamidating enzymes using radioactive amine substratesAnalytical Biochemistry, 1972
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970