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J. Biol. Chem., Vol. 265, Issue 35, 21971-21978, 12, 1990
HC Kim, MS Lewis, JJ Gorman, SC Park, JE Girard, JE Folk and SI Chung
We have isolated protransglutaminase E, the zymogen form of epidermal
transglutaminase E, from the skin of the adult guinea pig. This zymogen is
the source of the large majority of soluble transglutaminase activity of
skin. A molecular weight value for protransglutaminase E of 77,800 +/- 700,
estimated by sedimentation equilibrium, is in close agreement with the
apparent values determined by exclusion chromatography and by sodium
dodecyl sulfate-polyacrylamide gel electrophoresis. Treatment of the
proenzyme with dispase, proteinase K, trypsin, or thrombin produces active
enzyme. The enzyme, transglutaminase E, formed by the action of dispase,
was observed to exist in the native state as a molecule indistinguishable
in size from the zymogen. Under denaturing conditions, however, the enzyme
dissociates into two fragments with molecular weights of 50,000 and 27,000.
The observation that reducing agents are not needed for this dissociation
suggests a noncovalent association of the two peptide chains in the native
enzyme. Evidence that the catalytically essential - SH group of the enzyme
residues in the Mr 50,000 fragment and that only the Mr 27,000 fragment
possesses an unmasked amino terminus provides the basis for a proposed
model of zymogen activation. Whether the noncatalytic fragment plays a role
in catalysis is not known because separation of the fragments of native
enzyme was not achieved.
Protransglutaminase E from guinea pig skin. Isolation and partial characterization
Laboratory of Cellular Development and Oncology, National Institute of Dental Research, Bethesda, Maryland 20892.
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