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Biomedical subjects

M A Juillerat

Publications and source records attributed to M A Juillerat.

At least 19 recordsLinked to original sources
PubMed2001

Tomato (Lycopersicon esculentum) pectin methylesterase and polygalacturonase behaviors regarding heat- and pressure-induced inactivation.

The combined high pressure/thermal (HP/T) inactivation of tomato pectin methyl esterase (PME) and polygalacturonase (PG) was investigated as a possible alternative to thermal processing classically used for enzyme inactivation. The temperature and pressure ranges tested were from 60 degrees C to 105 degrees C, and from 0.1 to 800 MPa, respectively. PME, a heat-labile enzyme at ambient pressure, is dramatically stabilized against thermal denaturation at pressures above atmospheric and up to 500-600 MPa. PG, however, is very resistant to thermal denaturation at 0.1 MPa, but quickly and easily inactivated by combinations of moderate temperatures and pressures. Selective inactivation of either PME or PG was achieved by choosing proper combinations of P and T. The inactivation kinetics of these enzymes was measured and described mathematically over the investigated portion of the P/T plane. Whereas medium composition and salinity had little influence on the inactivation rates, PME was found less sensitive to both heat and pressure when pH was raised above its physiological value. PG, on the other hand, became more labile at higher pH values. The results are discussed in terms of isoenzymes and other physicochemical features of PME and PG.

Bioreactors↗
PubMed2000

Primary structure of the abundant seed albumin of Theobroma cacao by mass spectrometry.

The most abundant albumin present in seeds of Theobroma cacao was purified to apparent homogeneity as judged by high-performance liquid chromatography/electrospray ionization mass spectrometry (HPLC/ESI-MS), sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and NH(2)-terminal sequence analysis. Tryptic peptide mass fingerprinting of the purified protein by HPLC/ESI-MS showed the presence of 16 masses that matched the expected tryptic peptides corresponding to 95% of the translated amino acid sequence from the cDNA of the 21 kDa cocoa albumin. Collision-induced dissociation MS/MS analysis of the C-terminal peptide isolated from the CNBr cleavage products provided unequivocal evidence that the mature cocoa albumin protein is nine amino acid residues shorter than expected from the reported cDNA of its corresponding gene. The experimentally determined M(r) value of 20234 was in excellent agreement with the truncated version of the amino acid sequence. The purified cocoa albumin inhibited the catalytic activities of bovine trypsin and chymotrypsin. The inhibition was stoichiometric with 1 mol of trypsin or chymotrypsin being inhibited by 1 mol of inhibitor with apparent dissociation constants (K(i)) of 9.5 x 10(-8) and 2. 3 x 10(-6) M, respectively, for inhibitor binding at pH 8.5 and 37 degrees C. No inhibition of the catalytic activities of subtilisin, papain, pepsin, and cocoa endoproteases was detected under their optimal reaction conditions.

Albumins↗
PubMed1997

Bioavailability in infants of iron from infant cereals: effect of dephytinization.

Iron bioavailability from an infant cereal made of wheat flour with a low extraction rate (70%) and cow milk was measured in infants by using a stable-isotope technique. A dephytinized infant cereal was prepared by adding commercial phytase during manufacture, resulting in degradation of 88% of the native phytic acid. Paired comparisons were made to evaluate the effect of phytic acid on iron bioavailability. Both infant cereals contained identical amounts of ascorbic acid and had a molar ratio of ascorbic acid to iron of 2:1. Iron was added as ferrous sulfate. No difference in iron bioavailability was observed in this study; the geometric mean was 8.7% (range: 3.8-16.9%) and 8.5% (range: 3.4-21.4%) from the cereal with native phytic acid (0.08% phytic acid) and the dephytinized cereal (0.01% phytic acid), respectively. Dephytinization of infant cereals containing a relatively low native phytic acid content and high amounts of ascorbic acid is thus unnecessary to ensure adequate bioavailability of iron.

6-Phytase↗
PubMed1997

The influence of different cereal grains on iron absorption from infant cereal foods.

Iron absorption from various cereal grains was evaluated in the present study to identify possible preferences for the preparation of infant weaning foods. In six separate studies, four radioiron absorption tests were performed in each of 57 volunteer subjects by using a sequential double-isotopic method. Serum ferritin concentration was used to adjust for the effect of differences in the iron status of subjects participating in separate studies. Identical commercial processing and test meal composition were used to evaluate iron absorption from 50 g cooked cereal prepared from rice, wheat, maize, oats, millet, and sweet or bitter quinoa. In an initial evaluation of cereals fortified with 2.5 mg Fe as FeSO4, geometric mean absorption values were uniformly < 1% for all cereals and were not significantly different. In subsequent studies, percentage iron absorption was enhanced by either eliminating the fortifying iron or adding 50 mg ascorbic acid to the test meal. The effect was similar for most of the cereals tested with a composite mean increase in absorption of 37% when fortifying iron was removed and 270% when ascorbic acid was added. There was a strong inverse correlation between iron absorption and the phytate content of different cereals. Except for a modestly lower absorption of iron from quinoa and a remarkably higher absorption from one lot of maize, we conclude that the type of cereal grain has little influence on iron bioavailability of infant cereals. On the other hand, modification in the milling and processing methods for cereal grains that reduce their content of phytic acid is likely to improve iron availability significantly.

Absorption↗
PubMed1996

The influence of different protein sources on phytate inhibition of nonheme-iron absorption in humans.

The inhibiting effect of phytate on nonheme-iron absorption from different protein sources was examined in human subjects using extrinsic radioiron labeling. A drink containing maltodextrose and corn oil was used as a control meal to which was added sufficient sodium phytate to provide 300 mg phytic acid and/or various protein sources. The proteins were selected to cover a broad range of effects on bioavailability and included egg white, meat, and phytate-free soy protein. When sodium phytate alone was added, there was a pronounced 83-90% reduction in mean absorption in separate studies with a composite average decline of 86%. Despite a wide range in absorption from meals containing the three protein sources, a remarkably similar relative inhibition was observed when sodium phytate was added. No significant difference in the inhibiting effect of phytate could be detected with additions ranging from the equivalent of 50-300 mg phytic acid to a meal containing egg white as the protein source. Our studies found no evidence that the inhibiting effect of phytate depends on the protein composition of the meal.

Absorption↗
PubMed1995

Manganese absorption in humans: the effect of phytic acid and ascorbic acid in soy formula.

The absorption of manganese from soy formula was studied in adult volunteers by extrinsic labeling of test meals with 54Mn, followed by whole-body retention measurements for approximately 30 d after intake. Eight subjects participated twice in each of the two studies, acting as his or her own control. Soy formula containing the native content of phytic acid was compared with a similar dephytinized formula: geometric mean manganese absorption increased 2.3-fold from 0.7% (range: 0.2-1.1%) to 1.6% (range: 1.0-7.2%) (P < 0.01) with the dephytinized formula. In addition, the effect of the ascorbic acid content of the phytic acid-containing formula was investigated. Manganese absorption was not influenced by an increase in the ascorbic acid from 625 mumol/L (110 mg/L) to 1250 mumol/L (220 mg/L): the geometric mean manganese absorption was 0.6% (range: 0.3-1.0%) and 0.6% (range: 0.3-1.1%), respectively. In conclusion, fractional manganese absorption was approximately doubled by the dephytinization of soy formula but was not influenced by an increase in the ascorbic acid content of a soy formula containing the native amount of phytic acid.

Adult↗
PubMed1994

Inhibitory effect of a soybean-protein--related moiety on iron absorption in humans.

The inhibitory effect of soybean protein isolates on nonheme-iron absorption was studied in 34 human subjects. Iron absorption was measured by using an extrinsic radioiron label in liquid-formula meals containing hydrolyzed corn starch, corn oil, and either egg white or a series of soybean-protein derivatives. The unmodified soybean-protein isolate markedly inhibited iron absorption. Percentage absorption was 19-fold higher when an extensively enzyme-hydrolyzed preparation with very little phytate was used as the protein source. Both the glycinin (11S) and conglycinin (7S) fractions of soybean protein were inhibitory to iron absorption. Dephytinization removed the inhibitory effect of the glycinin but not of the conglycinin fraction. We conclude that there are two major inhibitors of iron absorption in soybean-protein isolates, phytic acid and a protein-related moiety contained in the conglycinin (7S) fraction.

Absorption↗
PubMed1994

Iron bioavailability studied in infants: the influence of phytic acid and ascorbic acid in infant formulas based on soy isolate.

The influence of phytic acid and ascorbic acid content of soy formula on iron (Fe) bioavailability was investigated in infants by analysis of the incorporation of stable isotopes of Fe into red blood cells 14 d after administration using a double stable isotope technique. Paired comparisons were made with each infant acting as his or her own control. The geometric mean fractional Fe incorporation into red blood cells increased from 5.5 to 6.8% (p < 0.05) when soy formula with the native content of phytic acid was compared with a 83% dephytinized formula. A more pronounced effect was shown with soy formula containing no phytic acid; the mean fractional Fe incorporation increased from 3.9 (native phytic acid) to 8.7% (zero phytic acid; p < 0.001). A significant (p < 0.01) effect was also demonstrated when the Fe:ascorbic acid molar ratio in the native phytate-containing formula was increased from 1:2.1 to 1:4.2; mean fractional Fe incorporation increased from 5.9 to 9.6%. These results demonstrate that the Fe bioavailability from soy-based infant formulas can be similarly increased by either removing phytic acid or increasing the ascorbic acid content.

Ascorbic Acid↗
PubMed1992

Soy protein, phytate, and iron absorption in humans.

The effect of reducing the phytate in soy-protein isolates on nonheme-iron absorption was examined in 32 human subjects. Iron absorption was measured by using an extrinsic radioiron label in liquid-formula meals containing hydrolyzed corn starch, corn oil, and either egg white or one of a series of soy-protein isolates with different phytate contents. Iron absorption increased four- to fivefold when phytic acid was reduced from its native amount of 4.9-8.4 to less than 0.01 mg/g of isolate. Even relatively small quantities of residual phytate were strongly inhibitory and phytic acid had to be reduced to less than 0.3 mg/g of isolate (corresponding to less than 10 mg phytic acid/meal) before a meaningful increase in iron absorption was observed. However, even after removal of virtually all the phytic acid, iron absorption from the soy-protein meal was still only half that of the egg white control. It is concluded that phytic acid is a major inhibitory factor of iron absorption in soy-protein isolates but that other factors contribute to the poor bioavailability of iron from these products.

Absorption↗
PubMed1989

Tryptic phosphopeptides from whole casein. II. Physicochemical properties related to the solubilization of calcium.

Casein phosphopeptides (CPP) were produced by tryptic hydrolysis of sodium caseinate and further purified by precipitation and chromatography on QAE-Sephadex A-25. Their physico-chemical properties were compared with the properties of an enzymically dephosphorylated equivalent preparation (DPP). Binding of Ca2+ to the peptides was measured using a Ca selective electrode and was found to increase with pH and to show 1/1 stoicheiometry Ca/Porg in CPP at pH 6.5 and 7.6. Klotz plots indicated equivalent binding sites at these two pH values, but some heterogeneity was seen at pH 3.5. In contrast, DPP did not bind significant amounts of Ca2+. CPP effectively inhibited the formation of insoluble calcium phosphates at different Ca/P ratios. The effective CPP concentration was 10 mg/l and complete stability of calcium phosphate solutions was obtained at about 100 mg/l. This stabilizing effect was dependent on the presence of organic P.

Calcium↗
PubMed1987

Intramolecular flip between two alternative forms of complex formed from a heme fragment and apoprotein of horse cytochrome c.

The previous studies have shown that (a) noncovalent interactions of the ferro-heme fragment of residues 1-38 and apoprotein (1-104) of horse cytochrome c simultaneously and specifically form two isomeric complexes, types I and II resembling the native protein (the redundant residues flexibly protruding from the ordered structure); (b) the type II form but not type I appears to bind to CO; and (c) residues 39-55 are more flexible for type II form than type I (Parr, G. R., and Taniuchi, H. (1981) J. Biol. Chem. 256, 125-132). In the present study, we investigated 1) kinetics and thermodynamics of interconversion between type I and II forms of complex ferro-(1-38)-H.(1-104); 2) the properties of the CO binding population; 3) the rate of dissociation of complexes ferri- and ferro-(1-38)-H.(39-104) (mimicking type II form); and 4) thermal transition of the 695-nm absorption band and biological activity of complexes. The results indicate (a) interconversion between type I and II forms of complex ferro-(1-38)-H.(1-104) occurs without going through dissociation (t1/2 less than or equal to 12 min at 10 degrees C) and is associated with delta H (= -7.2 +/- 3.7 kcal/mol at 10 degrees C) favoring type I form and delta S (= 23 +/- 13 e.u. at 10 degrees C) favoring type II; (b) the CO-binding population correlates with type II; and (c) change from the ferrous to the ferric state of heme appears to perturb the thermodynamic relationship between type I and II forms. Interpreting the results and available evidence, we suggest that "intramolecular" flip between ferro-type I and ferro-type II forms would establish the Boltzmann distribution of these two distinctly different energy states, type I form having more strengthened interatomic interactions and type II more pronounced internal motion.

Animals↗
PubMed1986

Analysis of folding intermediates from the main toxin of Naja naja samarensis containing two blocked cysteines.

The formation of folding intermediates blocked by iodoacetate from the main toxin of Naja naja samarensis was monitored by FPLC and the populations were identified by amino acid analyses. We have determined conditions allowing for the highest yield in the populations with two blocked cysteines. The free cysteines remaining under these conditions were labeled with iodo[14C]acetate and localized by peptide mapping in one of the products isolated by ion-exchange chromatography (NT3III). We have also investigated the effects on the native-like characteristics of such molecules of an incubation at equilibrium with a mixture of cysteine and cystine. We find that many different molecular populations are present during the folding process and that disulfide exchanges allow for the reconstitution of native-like products having open disulfides even under strongly denaturing conditions.

Amino Acid Sequence↗
PubMed1986

A study on the role of evolutionarily invariant leucine 32 of cytochrome c.

To investigate the role of evolutionarily invariant leucine 32 of horse cytochrome c, analogs of residues 28-38, (28-38), each containing a substituted amino acid at positions 32 or 35 were synthesized using Merrifield's method. Position 35 is leucine in horse cytochrome c but replaced by nonpolar amino acids in some species. The ability of the analogs to bind to the two-fragment complex of ferri- or ferro heme fragment (1-25)H and apofragment (39-104) was measured using gel filtration and equilibrium dialysis. Replacement of leucine 32 with isoleucine, for example, increased the dissociation constant by more than 400-fold for the ferrous complex. In contrast, replacement of leucine 35 with isoleucine seems to increase it only by a small degree. Since both leucine 32 and leucine 35 are completely buried within the structure, hydrophobic interaction would not explain this striking difference. However, thermodynamic analyses and absorption spectra of the ferric complex have indicated that replacement with norvaline of leucine 32 increases both delta H and delta S (more positive) associated with formation of an intermediate three-fragment complex and decreases both delta H and delta S (more negative) associated with transformation from the intermediate to the ground state, resulting in weakening the methionine 80--S--heme-Fe bond formed in the latter step. Taking the results together with the fragment exchange studies on the ferrous complex and available evidence, we suggest that the interaction involving leucine 32 would be coupled not only with the methionine 80--S--heme-Fe bond but also with the energy state of other distant residues such as tryptophan 59, generating extra energy for modulating the binding of the complex, i.e. the force of folding. In contrast, leucine 35 would be less important even if it were involved in such coupling.

Amino Acid Sequence↗
PubMed1984

Reoxidation and renaturation studies on the main toxin of Naja naja samarensis.

The main toxin of Naja naja samarensis is a very small and rigid protein (Mr 6850, 8 cysteines). When fully reduced, it regains its native conformation by a mechanism involving a rapid cysteine oxidation and a slower, less temperature-dependent disulfide exchange. In a native-like form of the protein we observed a population whose cysteines were incompletely reoxidized. When intermediates with blocked cysteines were incubated with oxidized and reduced glutathione, the percentage of native-like molecules increased. These findings suggest a multiple folding pathway.

Amino Acids↗
PubMed1984

Antigenic sites of the nicotinic acetylcholine receptor cannot be predicted from the hydrophilicity profile.

The amino acid sequences of the polypeptide chains of the acetylcholine receptor have recently been published. From the hydrophilicity profiles, it has been proposed that residues 161-166 of the alpha-chain might be an important antigenic site. We have synthesised a peptide containing this sequence and raised antisera to it. Here we report that this peptide does not represent an important antigenic site on the molecule, and that this region is probably inaccessible to antibodies. Based on the known DNA sequences and hydrophilicity profiles of the receptor chains, we suggest that many regions of high hydrophilicity may represent inter-domain regions of proteins.

Amino Acid Sequence↗
PubMed1984

Differential effects of two anti-apo-cytochrome c-specific monoclonal antibodies on the function of apo-cytochrome c-specific murine T cell clones.

A murine monoclonal antibody (SJL 2-4) specific for the antigen apo-cytochrome c was shown to inhibit both antigen-induced proliferation and lymphokine secretion by an apo-cytochrome c-specific BALB/c helper T cell clone. The inhibition was specific because additional apo-cytochrome c-specific T cell clones were not inhibited by the same monoclonal antibody. Time course studies of the inhibition indicated that the initial 8 hr of contact between T cell clones and antigen-presenting cells were critical for activation of the T cell clones. Inhibition of T cell functions by antigen-specific antibodies appeared to correlate with the antibody-antigen binding constant because a second monoclonal antibody (Cyt-1-59), with identical specificity but with a lower affinity constant for apo-cytochrome c, had very little inhibitory effect on the proliferation or lymphokine secretion of apo-cytochrome c-specific T cell clones.

Animals↗
PubMed1983

Fine specificity of a BALB/c T cell clone directed against beef apo cytochrome c.

A BALB/c cloned T cell line directed against beef apo cytochrome c was shown to exhibit the Lyt-1+2- cell surface phenotype. The fine specificity of antigen recognition exhibited by the T cell clone was assessed by using a variety of peptide preparations obtained from cytochrome c of different sources. The peptide segment recognized by this T cell clone, in conjunction with I-A region gene products, appeared similar to that bound by a monoclonal antibody specific for beef apo cytochrome c derived from the same strain of mice.

Amino Acid Sequence↗