Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.4.24.11 (
CD10
)
9,792
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The preparations of
chymotrypsin C
(
EC 3.4.21.2
) and an acidic
endopeptidase
from porcine pancreas have been repeated using published procedures. The acidic
endopeptidase
showed lower activity than
chymotrypsin C
in all comparative experiments, but it was possible to precipitate a fraction from the acidic
endopeptidase
preparation which contained all the protein and was identical with
chymotrypsin C
. It is concluded that the acidic
endopeptidase
is identical with
chymotrypsin C
but it is contaminated by an inert non-protein material to which it is firmly bound. The formation of a precipitate, at low ionic strength, from mixtures of
chymotrypsin C
and elastase (EC 3.4.21.11) is independent of the availability of the active site of either enzyme.
...
PMID:The identity of the elastase-associated acidic endopeptidase and chymotrypsin C from porcine pancreas. 126 39
Chymotrypsin C is a bifunctional secretory-type serine protease in pancreas; besides proteolytical activity, it also exhibits a calcium-decreasing activity in serum. In this study, we purified activated
chymotrypsin C
from porcine pancreas, and identified its three active forms. Active
chymotrypsin C
was found to be different in the length of its 13-residue activation peptide due to carboxydipeptidase (present in the pancreas) degradation or autolysis of the activated
chymotrypsin C
itself, resulting in the removal of several C-terminus residues from the activation peptide. After limited
chymotrypsin C
cleavage with
endopeptidase
Lys C, several purified peptides were partially sequenced, and the entire cDNA sequence for porcine
chymotrypsin C
was cloned. Recombinant chymotrypsinogen C was successfully expressed in Escherichia coli cells as inclusion bodies. After refolding and activation with trypsin, the comparison of the recombinant
chymotrypsin C
with the natural form showed that their proteolytic and calcium-decreasing activities were at the same level. The successful expression of
chymotrypsin C
gene paves the way to further mutagenic structure-function studies.
...
PMID:Purification, cDNA cloning, and recombinant expression of chymotrypsin C from porcine pancreas. 2165 82
