Nutritional status of exclusively breastfeeding adolescents from northwest and central Mexico.
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Adolescent↗
Biomedical subjects
A M Calderón de la Barca
Publications and source records attributed to A M Calderón de la Barca.
Nutritional and clinical evaluation of a modified soy protein with covalently bound branched-chain amino acids in cirrhotic sprague-dawley rats.
Several studies suggested that branched-chain amino acids (BCAA) improve plasma amino acid imbalance as well as protein metabolism in patients with cirrhosis. However, commercial formulas supplemented with free BCAA have their limitations. We evaluated a modified soy protein diet with covalently bound BCAA (diet M) by comparing it with diets based on casein (diet C) or Hepatic Aid II (diet H; commercial formula) as protein sources. After 3 weeks of bile duct obstruction, 24 Sprague-Dawley rats divided into three groups received diets with 9% (w/w) protein/amino acids for 7 days. Nutritional and clinical parameters were determined. Nitrogen balance and weight gain (g)/protein intake (g) with diet M (0.19 +/- 0.31 and 1.33 +/- 1.43 g, respectively) were significantly higher (p < 0.05) than with diet H (-0.34 +/- 0.20 and -0.34 +/- 1.11 g), but comparable to those with diet C (0.04 +/- 0.38 and 0.20 +/- 0.93 g). Animals on diet M had a significantly (p < 0.05) increased plasma BCAA:aromatic amino acid ratio (1.8 +/- 0.3) as compared with those on diets H (1.3 +/- 0.1) and C (0.8 +/- 0.0). There were no significant differences in organ weight or liver function among the groups. We conclude that the BCAA-modified protein is an attractive option in the nutritional support of patients having cirrhosis.
Amino Acids↗
Energy intake and growth of breast-fed infants in two regions of Mexico.
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Breast Feeding↗
[Enzymatic modification of the functional, nutritional and sensorial properties of soybeans for special feeding].
Production of new protein-based products for special nutrition such as hypoallergenic infant formulas, fortified beverages and nutraceutics, require ideal ingredients. Protein ingredients were developed by enzymatic hydrolysis and methionine synthesis of soy protein. Hydrolysis was done at 4% (w/v) using porcine pancreatic enzymes (4% w/w), 50 degrees C, 6 h and pH 8. After drying powder was resuspended (20% w/v) and incubated with 7.6% (w/w) methionine methyl-ester, 1% (w/w) chymotrypsin and 3 M glycerol, 37 degrees C, 3 h and pH 7. Hydrolysates were fractionated by ultrafiltration (UF) before and after enrichment (E): FI > 10, 10 > FII > 3 and 3 > FIII > 1 kDa. Functional properties, amino acid content, anti-physiological factor activities and antigenicity were assayed for all the UF fractions and the soybean meal. Protein quality bioassay and sensorial test of an non-enriched fraction and an enriched fraction were performed. Functional properties were positively modified by hydrolysis and synthesis by using a minimum time and methionine added for the last reaction. After UF all the fractions under 10 kDa showed 100% solubility (pH 4 and 7), good clarity, acceptable foam capacity and negligible antigenicity and antiphysiological activities. Additionally, methionine enrichment enhanced their nutritional value, upgrading sulfur amino acid requirements for infants and adults. Because functionality and nutritional value FIII-E could be used for hypoallergenic infant formulas, FII-E for fortified soluble formulas and nutraceutics and FI-E for a semi-solid baby food.
Amino Acids↗
Immunological and functional properties of the exudate gum from northwestern Mexican mesquite (Prosopis spp.) in comparison with gum arabic.
A comparison between the fine structural features of exudate gum from mesquite (Prosopis spp.) indigenous to NW Mexico and commercial gum arabic from Acacia spp. was achieved by means of immunological techniques. Their functional properties were compared from the ability to form oil-in-water emulsions and encapsulate cold press orange peel essential oil by spray drying. Fine comparison of the antigenic compounds in both materials against polyclonal rabbit antibodies, showed that the carbohydrate-rich components with slow mobility of mesquite gum are closely related to the faster ones of gum arabic. Also, close identity was observed for the components in the proteic fraction of both gums. Similar tannin concentrations were found in both materials (approximately 0.43%) with only dark coloured samples bearing higher amounts (approximately 1.9%). Gum arabic retained nearly 100% of the quantity of orange peel essential oil emulsified in water before spray drying, while mesquite gum did so for 90.6% of the citrus oil. From these results it is believed that mesquite gum might be a suitable replacement of gum arabic in arid regions of the world were Prosopis trees have widespread occurrence.
Animals↗
Hydrophobic interactions between gliadin and proteins and celiac disease.
Gliadin-protein interaction and its relationship to the pathogenesis hypotheses of celiac disease was investigated. Wheat germ agglutinin was not immunodetected in gliadin preparations. Peptic-tryptic gliadin digest was used to study the gliadin-protein interactions by crossed immunoelectrophoresis and affinity blotting. Biotinylated gliadin digest interacted with IgG and bovine serum albumin but not with several glycoproteins. Since albumin and IgG light chains are not glycosylated, this interaction is not lectin-like, neither completely immunological because of recognition of the IgG Fc fraction. Immobilized and boiled IgG was not recognized by gliadin digest as a lectin. Gliadin digest fractions from T-gel chromatography reduced the fluorescence intensity of cis-parinaric acid bound to albumin. The gliadin-protein interaction is not lectin-like or completely immunological but hydrophobic. Hydrophobicity of gliadins may contribute to the pathogenic events that result in celiac disease.
Celiac Disease↗
Affinity methods with lectins: a tool to identify canine alkaline phosphatase isoenzymes.
Affinity methods were used to characterize selective interactions of alkaline phosphatase (ALP) isoenzymes from different dog tissues with lectins. Specific lectins were used to identify liver, intestinal and steroid-induced ALP isoenzymes in serum from dogs with Cushing syndrome or steroid-treated dogs. For the first approach, 12 lectins were assayed by affinity dots. Selective interactions were found among wheat germ agglutinin (WGA), jacalin, con A (concanavalin A) and Helix pomatia agglutinin (HPA) and several ALP-containing samples. These four reactive lectins were assayed by line electrophoresis with lectins in holes. A strong reactivity of con A with all isoenzymes was found, although the patterns were different. WGA interacted with intestinal, bone marrow extracts and Cushing syndrome serum. Jacalin changed the electrophoretic patterns of intestinal and liver ALP, and Cushing serum. Finally, by crossed electrophoresis with lectins in gels, it was possible to distinguish among hepatic or intestinal ALPs and the steroid-induced isoenzyme in serum. Affinity electrophoresis with lectins provided a clear separation and identification of the different dog ALP isoenzymes.
Alkaline Phosphatase↗
Interactions between listeriae and lectins.
Interactions between members of the genus Listeria and lectins are described. L. monocytogenes was shown to be heterogenous with respect to agglutination by lectins. L. monocytogenes serotype 4b had a pattern of lectin binding distinct from the other listeriae. Titration of the listeriae with lectins proved to be useful in further distinguishing serotype 4b. The results show that lectins may provide useful probes as diagnostic reagents for listeriae.
Agglutination↗