Abstract
Dipeptidyl peptidase IV (DPP IV, E.C.3.4.14.5) is a glycoprotein present in high activities in the plasma membranes of mammalian tissues. Although the enzyme has been investigated in detail for several years, its biological role remains still obscure. Because of the specificity for N-terminal Gly-Pro-dipeptides, its possible role in collagen metabolism was suggested (1). It could be shown, that DPP IV is involved in the interaction of hepatocytes with the extracellular matrix (2). In Morris hepatoma 7777 the specific activity of plasma membrane DPP IV is reduced to about 3% (3), which is concomitant with a decreased cell-substratum adhesion of hepatoma cells (4). In addition to the membrane-bound enzyme, about 15% of total DPP IV activity in liver and about 50% of the total DPP IV activity in hepatoma is found in the soluble fraction (5). This observation prompted the present study on the relationship and differences between the enzyme of liver and hepatoma. The comparison of DPP IV from various sources was carried out with monoclonal antibodies directed against different epitopes of the enzyme.
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© 1988 Plenum Press, New York
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Hartel, S., Hanski, C., Neumeier, R., Gossrau, R., Reutter, W. (1988). Characterization of Different Forms of Dipeptidyl Peptidase IV from Rat Liver and Hepatoma by Monoclonal Antibodies. In: Hörl, W.H., Heidland, A. (eds) Proteases II. Advances in Experimental Medicine and Biology, vol 240. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-1057-0_25
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DOI: https://doi.org/10.1007/978-1-4613-1057-0_25
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