The high molecular weight arylamidase-alkaline phosphatase-complex from rat kidney microsomes [1] was carefully dissociated by means of treatment with several hydrolytic enzymes or by acidification. Trypsin, chymotrypsin and pronase cause a selective solubilization of the enzymes discernible at their different electrophoretic mobility in polyacrylamide gel. The lower migrating zone represents phosphatase, the faster migrating zone shows arylamidase activity (molecular weights 180,000 and 172,000, respectively). Incubation of the complex with papain, lipase, neuraminidase or hyaluronidase and incubation at acid conditions (pH optimum 5.0) in the absence of any enzyme also yields in the appearance of two protein bands. In contrast to the alkaline hydrolases the acid hydrolases, the pH 5-treatment and with a certain degree also the lipase liberate a second arylamidase zone lying in the phosphatese containing zone during polyacrylamide gel electrophoresis. Treatment with SDS and subsequent SDS-polyacrylamide gel electrophoresis also results in a dissociation of the complex, but only in one protein fragement (approx, molecular weight 205,000).
Kleine
R
R
Physiologisch-chemisches Institut der Martin-Luther-Universität Halle/S., 1, Hollystrasse, DDR
Schubert
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J
Dissoziation des mikrosomalen arylamidase-alkalischen phosphatase-komplexes aus rattennieren.