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(Received for publication, April 12, 1996, and in revised form, October 14, 1996)
From the Department of Biochemistry and Molecular Biology and
Graduate Program in Molecular and Cellular Biology, University of
Massachusetts, Amherst, Massachusetts 01003
A cysteine protease that initiates degradation of
vitellin (Vt) in the orthopteran Blattella germanica, and
its proprotease precursor, were purified from yolk and partially
characterized. The protease, purified 300-fold, contains three peptides
of Mr 27,000, 29,000, and 31,000. A comparison
of the purified enzyme's action pattern on Vt in vivo and
in vitro confirmed its role in Vt processing.
Protease-deficient yolk (day 0 postovulation) contained peptides of
Mr 35,500, 37,000, 39,000, and 41,000, which
were absent from yolk with protease activity. These were replaced by three peptides of approximately Mr 29,000, at
days 2-3, the same time in development that protease expression and
acidification of yolk granules occur (Nordin, J. H., Beaudoin, E. L.,
and Liu, X. (1991) Arch. Insect Biochem. Physiol. 18, 177-192). Acidification of purified proprotease converted it to three
peptides of approximately Mr 29,000 with
cysteine protease activity. This conversion also required participation
of a cysteine protease. Activated proprotease had the same pH activity
profile, susceptibility to inhibitors, and cathepsin classification (L)
as the protease. These results indicate that the Vt-processing protease
is derived from a proprotease, which is activated in vivo
by a developmentally regulated decrease in intragranular pH.
Volume 271, Number 52,
Issue of December 27, 1996
pp. 33344-33351
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
PURIFICATION AND PARTIAL CHARACTERIZATION OF THE ENZYME AND THE
PROENZYME
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