35 research outputs found
Bank consolidation and financial stability revisited: Evidence from Indonesia
This paper extends prior literature on the link between consolidation and stability in banking using a single country setting. From a sample of Indonesian commercial banks over the 2010-2015 time span, we construct the Lerner index as a measure of bank market power due to consolidation. Our empirical results document that higher bank market power tends to reduce insolvency risk and increase capital ratios. A deeper analysis however reveals that higher market power is detrimental for financial stability in state-owned banks and small private-owned banks. We therefore highlight that although consolidation among state-owned banks reduces cost inefficiency as in Hadad et al. (2013), further efforts to reduce state-owned banks' market power are necessary after consolidation. This paper also suggests that strengthening market power in large private-owned banks, but encouraging competition in small private-owned banks to reduce market power, are of particular importance for financial stability. JEL Code: G21, G2
Two Traditional Maize Inbred Lines of Contrasting Technological Abilities Are Discriminated by the Seed Flour Proteome
The seed proteome of two traditional
maize inbred lines (pb269 and pb369) contrasting in grain hardness
and in preferable use for bread-making was evaluated. The pb269 seeds,
of flint type (i.e., hard endosperm), are preferably used by manufacturers,
while pb369 (dent, soft endosperm) is rejected. The hypothesis that
the content and relative amounts of specific proteins in the maize
flour are relevant for such discrimination of the inbred lines was
tested. The flour proteins were sequentially extracted following the
Osborne fractionation (selective solubilization), and the four Osborne
fractions were submitted to two-dimensional electrophoresis (2DE).
The total amount of protein extracted from the seeds was not significantly
different, but pb369 flour exhibited significantly higher proportions
of salt-extracted proteins (globulins) and ethanol-extracted proteins
(alcohol-soluble prolamins). The proteome analysis allowed discrimination
between the two inbred lines, with pb269 demonstrating higher heterogeneity
than pb369. From the 967 spots (358 common to both lines, 208 specific
to pb269, and 401 specific to pb369), 588 were submitted to mass spectrometry
(MS). Through the combined use of trypsin and chymotrypsin it was
possible to identify proteins in 436 spots. The functional categorization
in combination with multivariate analysis highlighted the most discriminant
biological processes (carbohydrate metabolic process, response to
stress, chitin catabolic process, oxidation–reduction process)
and molecular function (nutrient reservoir activity). The inbred lines
exhibited quantitative and qualitative differences in these categories.
Differences were also revealed in the amounts, proportions, and distribution
of several groups of storage proteins, which can have an impact on
the organization of the protein body and endosperm hardness. For some
proteins (granule-bound starch synthase-1, cyclophilin, zeamatin),
a change in the protein solubility rather than in the total amount
extracted was observed, which reveals distinct in vivo associations
and/or changes in binding strength between the inbred lines. Our approach
produced information that relates protein content, relative protein
content, and specific protein types to endosperm hardness and to the
preferable use for “broa” bread-making
Two Traditional Maize Inbred Lines of Contrasting Technological Abilities Are Discriminated by the Seed Flour Proteome
The seed proteome of two traditional
maize inbred lines (pb269 and pb369) contrasting in grain hardness
and in preferable use for bread-making was evaluated. The pb269 seeds,
of flint type (i.e., hard endosperm), are preferably used by manufacturers,
while pb369 (dent, soft endosperm) is rejected. The hypothesis that
the content and relative amounts of specific proteins in the maize
flour are relevant for such discrimination of the inbred lines was
tested. The flour proteins were sequentially extracted following the
Osborne fractionation (selective solubilization), and the four Osborne
fractions were submitted to two-dimensional electrophoresis (2DE).
The total amount of protein extracted from the seeds was not significantly
different, but pb369 flour exhibited significantly higher proportions
of salt-extracted proteins (globulins) and ethanol-extracted proteins
(alcohol-soluble prolamins). The proteome analysis allowed discrimination
between the two inbred lines, with pb269 demonstrating higher heterogeneity
than pb369. From the 967 spots (358 common to both lines, 208 specific
to pb269, and 401 specific to pb369), 588 were submitted to mass spectrometry
(MS). Through the combined use of trypsin and chymotrypsin it was
possible to identify proteins in 436 spots. The functional categorization
in combination with multivariate analysis highlighted the most discriminant
biological processes (carbohydrate metabolic process, response to
stress, chitin catabolic process, oxidation–reduction process)
and molecular function (nutrient reservoir activity). The inbred lines
exhibited quantitative and qualitative differences in these categories.
Differences were also revealed in the amounts, proportions, and distribution
of several groups of storage proteins, which can have an impact on
the organization of the protein body and endosperm hardness. For some
proteins (granule-bound starch synthase-1, cyclophilin, zeamatin),
a change in the protein solubility rather than in the total amount
extracted was observed, which reveals distinct in vivo associations
and/or changes in binding strength between the inbred lines. Our approach
produced information that relates protein content, relative protein
content, and specific protein types to endosperm hardness and to the
preferable use for “broa” bread-making
Two Traditional Maize Inbred Lines of Contrasting Technological Abilities Are Discriminated by the Seed Flour Proteome
The seed proteome of two traditional
maize inbred lines (pb269 and pb369) contrasting in grain hardness
and in preferable use for bread-making was evaluated. The pb269 seeds,
of flint type (i.e., hard endosperm), are preferably used by manufacturers,
while pb369 (dent, soft endosperm) is rejected. The hypothesis that
the content and relative amounts of specific proteins in the maize
flour are relevant for such discrimination of the inbred lines was
tested. The flour proteins were sequentially extracted following the
Osborne fractionation (selective solubilization), and the four Osborne
fractions were submitted to two-dimensional electrophoresis (2DE).
The total amount of protein extracted from the seeds was not significantly
different, but pb369 flour exhibited significantly higher proportions
of salt-extracted proteins (globulins) and ethanol-extracted proteins
(alcohol-soluble prolamins). The proteome analysis allowed discrimination
between the two inbred lines, with pb269 demonstrating higher heterogeneity
than pb369. From the 967 spots (358 common to both lines, 208 specific
to pb269, and 401 specific to pb369), 588 were submitted to mass spectrometry
(MS). Through the combined use of trypsin and chymotrypsin it was
possible to identify proteins in 436 spots. The functional categorization
in combination with multivariate analysis highlighted the most discriminant
biological processes (carbohydrate metabolic process, response to
stress, chitin catabolic process, oxidation–reduction process)
and molecular function (nutrient reservoir activity). The inbred lines
exhibited quantitative and qualitative differences in these categories.
Differences were also revealed in the amounts, proportions, and distribution
of several groups of storage proteins, which can have an impact on
the organization of the protein body and endosperm hardness. For some
proteins (granule-bound starch synthase-1, cyclophilin, zeamatin),
a change in the protein solubility rather than in the total amount
extracted was observed, which reveals distinct in vivo associations
and/or changes in binding strength between the inbred lines. Our approach
produced information that relates protein content, relative protein
content, and specific protein types to endosperm hardness and to the
preferable use for “broa” bread-making
Two Traditional Maize Inbred Lines of Contrasting Technological Abilities Are Discriminated by the Seed Flour Proteome
The seed proteome of two traditional
maize inbred lines (pb269 and pb369) contrasting in grain hardness
and in preferable use for bread-making was evaluated. The pb269 seeds,
of flint type (i.e., hard endosperm), are preferably used by manufacturers,
while pb369 (dent, soft endosperm) is rejected. The hypothesis that
the content and relative amounts of specific proteins in the maize
flour are relevant for such discrimination of the inbred lines was
tested. The flour proteins were sequentially extracted following the
Osborne fractionation (selective solubilization), and the four Osborne
fractions were submitted to two-dimensional electrophoresis (2DE).
The total amount of protein extracted from the seeds was not significantly
different, but pb369 flour exhibited significantly higher proportions
of salt-extracted proteins (globulins) and ethanol-extracted proteins
(alcohol-soluble prolamins). The proteome analysis allowed discrimination
between the two inbred lines, with pb269 demonstrating higher heterogeneity
than pb369. From the 967 spots (358 common to both lines, 208 specific
to pb269, and 401 specific to pb369), 588 were submitted to mass spectrometry
(MS). Through the combined use of trypsin and chymotrypsin it was
possible to identify proteins in 436 spots. The functional categorization
in combination with multivariate analysis highlighted the most discriminant
biological processes (carbohydrate metabolic process, response to
stress, chitin catabolic process, oxidation–reduction process)
and molecular function (nutrient reservoir activity). The inbred lines
exhibited quantitative and qualitative differences in these categories.
Differences were also revealed in the amounts, proportions, and distribution
of several groups of storage proteins, which can have an impact on
the organization of the protein body and endosperm hardness. For some
proteins (granule-bound starch synthase-1, cyclophilin, zeamatin),
a change in the protein solubility rather than in the total amount
extracted was observed, which reveals distinct in vivo associations
and/or changes in binding strength between the inbred lines. Our approach
produced information that relates protein content, relative protein
content, and specific protein types to endosperm hardness and to the
preferable use for “broa” bread-making
Two Traditional Maize Inbred Lines of Contrasting Technological Abilities Are Discriminated by the Seed Flour Proteome
The seed proteome of two traditional
maize inbred lines (pb269 and pb369) contrasting in grain hardness
and in preferable use for bread-making was evaluated. The pb269 seeds,
of flint type (i.e., hard endosperm), are preferably used by manufacturers,
while pb369 (dent, soft endosperm) is rejected. The hypothesis that
the content and relative amounts of specific proteins in the maize
flour are relevant for such discrimination of the inbred lines was
tested. The flour proteins were sequentially extracted following the
Osborne fractionation (selective solubilization), and the four Osborne
fractions were submitted to two-dimensional electrophoresis (2DE).
The total amount of protein extracted from the seeds was not significantly
different, but pb369 flour exhibited significantly higher proportions
of salt-extracted proteins (globulins) and ethanol-extracted proteins
(alcohol-soluble prolamins). The proteome analysis allowed discrimination
between the two inbred lines, with pb269 demonstrating higher heterogeneity
than pb369. From the 967 spots (358 common to both lines, 208 specific
to pb269, and 401 specific to pb369), 588 were submitted to mass spectrometry
(MS). Through the combined use of trypsin and chymotrypsin it was
possible to identify proteins in 436 spots. The functional categorization
in combination with multivariate analysis highlighted the most discriminant
biological processes (carbohydrate metabolic process, response to
stress, chitin catabolic process, oxidation–reduction process)
and molecular function (nutrient reservoir activity). The inbred lines
exhibited quantitative and qualitative differences in these categories.
Differences were also revealed in the amounts, proportions, and distribution
of several groups of storage proteins, which can have an impact on
the organization of the protein body and endosperm hardness. For some
proteins (granule-bound starch synthase-1, cyclophilin, zeamatin),
a change in the protein solubility rather than in the total amount
extracted was observed, which reveals distinct in vivo associations
and/or changes in binding strength between the inbred lines. Our approach
produced information that relates protein content, relative protein
content, and specific protein types to endosperm hardness and to the
preferable use for “broa” bread-making
Two Traditional Maize Inbred Lines of Contrasting Technological Abilities Are Discriminated by the Seed Flour Proteome
The seed proteome of two traditional
maize inbred lines (pb269 and pb369) contrasting in grain hardness
and in preferable use for bread-making was evaluated. The pb269 seeds,
of flint type (i.e., hard endosperm), are preferably used by manufacturers,
while pb369 (dent, soft endosperm) is rejected. The hypothesis that
the content and relative amounts of specific proteins in the maize
flour are relevant for such discrimination of the inbred lines was
tested. The flour proteins were sequentially extracted following the
Osborne fractionation (selective solubilization), and the four Osborne
fractions were submitted to two-dimensional electrophoresis (2DE).
The total amount of protein extracted from the seeds was not significantly
different, but pb369 flour exhibited significantly higher proportions
of salt-extracted proteins (globulins) and ethanol-extracted proteins
(alcohol-soluble prolamins). The proteome analysis allowed discrimination
between the two inbred lines, with pb269 demonstrating higher heterogeneity
than pb369. From the 967 spots (358 common to both lines, 208 specific
to pb269, and 401 specific to pb369), 588 were submitted to mass spectrometry
(MS). Through the combined use of trypsin and chymotrypsin it was
possible to identify proteins in 436 spots. The functional categorization
in combination with multivariate analysis highlighted the most discriminant
biological processes (carbohydrate metabolic process, response to
stress, chitin catabolic process, oxidation–reduction process)
and molecular function (nutrient reservoir activity). The inbred lines
exhibited quantitative and qualitative differences in these categories.
Differences were also revealed in the amounts, proportions, and distribution
of several groups of storage proteins, which can have an impact on
the organization of the protein body and endosperm hardness. For some
proteins (granule-bound starch synthase-1, cyclophilin, zeamatin),
a change in the protein solubility rather than in the total amount
extracted was observed, which reveals distinct in vivo associations
and/or changes in binding strength between the inbred lines. Our approach
produced information that relates protein content, relative protein
content, and specific protein types to endosperm hardness and to the
preferable use for “broa” bread-making
Peptides from βPG identified in <i>Arabidopsis</i>, cannabis and maize.
<p>Peptides from βPG identified in <i>Arabidopsis</i>, cannabis and maize.</p
MS/MS spectrum of the precursor at m/z 1548.6924.
<p>The peptide was identified as SFNEGTDKFTGYGK from the Cannabis sativa polygalacturonase non-catalytic protein (NCBI EST database GI:156080210). The upper panel shows the MS/MS spectrum with y- and b-ions indicated respectively in red and green. The one-letter code is used for the amino acids and dF indicates a didehydrophenylalanine. The lower spectra illustrate the specificity of the modification. While no mass shift is observed for the Phe closest to the N-terminus, illustrated by the lack of secondary peak at 233 for the b2-ion shown in the left panel, the more C-terminal Phe is completely modified as illustrated for the y6- and b9-fragment in the central and right lower panel.</p
From Tolerance to Acute Metabolic Deregulation: Contribution of Proteomics To Dig into the Molecular Response of Alder Species under a Polymetallic Exposure
<i>Alnus</i> spp. are actinorhizal trees commonly found
in wet habitats and able to grow effectively in soil slightly contaminated
with metal trace- elements. Two clones belonging to two <i>Alnus</i> species, namely, <i>A. incana</i> and <i>A. glutinosa</i>, were grown in hydroponics and exposed for 9 weeks to a Cd + Ni
+ Zn polymetallic constraint. Although responding by a similar decrease
in total biomass production, the proteomic analysis associated with
the study of various biochemical parameters including carbohydrate
and mineral analyses revealed that the two clones have a distinct
stress-responsive behavior. All parameters indicated that the roots,
the organ in direct contact with the media, are more affected than
the leaves. In fact, in <i>A. glutinosa</i> the response
was almost completely confined to the roots, whereas many proteins
change significantly in the roots and in the leaves of the treated <i>A. incana</i>. In both clones, the changes affected a broad
range of metabolic processes such as redox regulation and energy metabolism
and induced the production of pathogenesis-related proteins. In particular,
changes in the accumulation of bacterial proteins that were not identified
as coming from the known symbionts of <i>Alnus</i> were
reported. Further investigation should be performed to identify their
origin and exact role in the plant response to the polymetallic exposure
tested here