... alignment of the
interdomain and autolysis loops of
mammalian chymotrypsins and trypsins.
The enzyme that was used in this study, rat
chymotrypsin B, is highlighted by bold type.
The loops are boxed and ... 2).
Finally it is of interest regarding the in vivo mechanism of
inactivation, that chymotrypsin and trypsin, mixed in
concentration ratios close to thos...
... rate of
amylopectin synthesis. The increase in crystallinity wit-
nessed during these first 12 h is in line with the high rates
observed for amylopectin synthesis. However between 12
and 58 h the ... amylose continues to
accumulate at the final stage of starch synthesis in the
absence of concomitant amylopectin synthesis (reviewed in
[41]).
In vitro
synthesis of am...
... present-day N-terminal domain. Conse-
quently, the salt bridge may play an important role in the
proper attachment of the N- and C-terminal domains
during protein folding.
Several other residues ... an
invariantpartofallthreeclassesoftheplantperoxidase
superfamily [44]. This motif (shown in grey shading in
Fig. 1) includes Ser96 and Asp99 located at the beginning
of heli...
... (G66, R68
and G74) of Calb I–II lack the side-chain oxygens expected
to provide calcium-binding ligands. The absence of
calcium-binding to the EF-hand II motif of Calb has been
shown in the individual ... for
the full-length proteins.
Keywords: calretinin; calcium; calbindin D
28k
; EF-hand;
NMR secondary structure.
Calretinin (CR) and calbindin D
28k
(Calb) are homologo...
... 2002
Extent of proteolysis as a function of temperature, time,
and enzyme concentration
BLG appeared to be virtually insensible to hydrolysis by
either trypsin or chymotrypsin in the absence of a thermal
unfolding ... of these hydrophobic residues are pointing
inwards in the native protein structure, in which they line the
hydrophobic cavity t hat characterizes all lip...
... the
activity of the enzyme was measured by the dinitrosalicylic
acid method.
Inhibition of the enzyme activity by glucose, maltose and
cyclohexaamylose
For the study of the enzyme inhibition by glucose, ... by the inhibitors of the enzymatic activity.
Therefore the iodine staining method is well suited for
extensive kinetic analyses of purified b-amylases.
Stabili...
... probably represents fragment 21–124, as in Fig. 5A.
Quantification of the proteolytic susceptibility of
RNase A. To gain further insight into the changes of the
proteolytic susceptibility of RNase ... CD spectra in the
far-UV region, on the other hand, indicate a detectable
increase in the content of secondary structure only after the
disruption of the native...
... both
O6 and N7 (Fig. 1C). The 2¢OH of the ribose is hydro-
gen bonded to the main chain and the side chain of
Asp142 (Fig. 1C). Both hydroxyl groups of the ribose
are involved in coordinating a ... com-
pared to the spectrophotometric methods.
Because the enzymatic activity of PRTFDC1
towards hypoxanthine and guanine is only 0.26% and
0.09%, respectively, of...
... structural role in the proper folding
and disulfide bonding in insulin [2]. After proinsulin
cleavage, it is released to the blood together with insu-
lin in equimolar amounts. The 31-residue peptide ... distribu-
tion of 100 l
M proinsulin C-peptide in the
presence of divalent Ca
2+
and Mg
2+
ions
under native conditions (B), and of 100 l
M
C-peptide in the...
... in dual-flavin
enzymes because of a number of factors, including the
k
1
and k
2
of K
eq
A possibly being in uenced by changes
in the FAD and FMN reduction state or by changes
in NADP(H)-binding ... unclear at this point,
but may certainly involve apparent differences in their
CT and autoinhibitory insert elements, or elsewhere in
the enzyme.
Changing the set poi...