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At least 73 records · Page 4Linked to original sources

Comparative flatulence activity of beans and bean fractions for man and the rat.

To evaluate H2 production in the rat after ingestion of legume products as a predictive bioassay of their flatulence activity for man, responses of man and the rat to (1) a bland formula diet, (2) cooked California Small White bean (CSW) solids, (3) 70% ethanol extract of (2), (4) oligosaccharide fraction of (3), (5) non-protein nitrogen fraction of (3), and (6) combination of (4) and (5) were compared. Six human subjects were fed an 800 kcal breakfast of (1) or containing the amount of a test item equivalent to 100 g CSW. Each subject received all items once plus a single replicate of three items at the rate of one per week in random order. Total flatus volume, H2, CO2, and CH4 volumes and breath H2 concentration were measured for the interval 2.5 to 8.5 hours after breakfast. Young rats in metabolic chambers received known amounts of items 2 to 6 mixed with a bland basal diet. H2 trapped in the chambers was measured after 20 hours. Correlation of rat H2 and to human breath H2 measurements and flatus gas volumes were significant and positive except for negative correlation with flatus methane volume. Measurement of hydrogen production in the rat has potential for a predictive bioassay for flatulence in man.

Adult↗

A root-specific bZIP transcription factor is responsive to water deficit stress in tepary bean (Phaseolus acutifolius) and common bean (P. vulgaris).

Root cDNA libraries were differentially screened to isolate water deficit-responsive transcripts in the relatively drought-resistant plant tepary bean (Phaseolus acutifolius). A novel root-specific, water deficit-responsive transcript was identified and predicted to encode a bZIP transcription factor. The orthologous form of this gene was isolated from the drought-sensitive P. vulgaris and the patterns of expression of these genes compared. These genes have predicted amino acid sequences in the bZIP domain that are 64% similar to a soybean bZIP protein. There were three amino acid differences between the P. acutifolius bZIP and the P. vulgaris gene product. Both species transcribed this gene in a root-specific and water deficit-responsive manner. The cell-specific pattern of expression for the gene was determined using in situ hybridization and immunolocalization. Two tissues in the root accumulated the protein: epidermis and phloem. The nuclear localization of this protein was determined by electron microscopy. The bZIP protein accumulated in the nuclei of both the epidermal cell and the vascular cell in response to water deficit stress in both species in a similar manner.

Adaptation, Physiological↗

Solution conformation of several free tRNALeu species from bean, yeast and Escherichia coli and interaction of these tRNAs with bean cytoplasmic Leucyl-tRNA synthetase. A phosphate alkylation study with ethylnitrosourea.

The solution conformation of eight leucine tRNAs from Phaseolus vulgaris, baker's yeast and Escherichia coli, characterized by long variable regions, and the interaction of four of them with bean cytoplasmic leucyl-tRNA synthetase were studied by phosphate mapping with ethylnitrosourea. Phosphate reactivities in the variable regions agree with the existence of RNA helices closed by miniloops. At the junction of these regions with the T-stem, phosphate 48 is strongly protected, in contrast to small variable region tRNAs where P49 is protected. The constant protection of P22 is another characteristics of leucine tRNAs. Conformational differences between leucine isoacceptors concern the anticodon region, the D-arm and the variable region. In several parts of free tRNALeu species, e.g. in the T-loop, phosphate reactivities are similar to those found in tRNAs of other specificities, indicating conformational similarities among tRNAs. Phosphate alkylation of four leucine tRNAs complexed to leucyl-tRNA synthetase indicates that the 3'-side of the anticodon stem, the D-stem and the hinge region between the anticodon and D-stems are in contact with the plant enzyme.

Alkylation↗

Evidence that the castor bean allergens are the albumin storage proteins in the protein bodies of castor bean.

The well characterized castor bean (Ricinus communis L.) allergens were identified as the low molecular weight albumin storage proteins in the matrix of the protein bodies in the endosperm. The methods of identification involved molecular weight estimation, amino acid composition, stability at 100 degrees C, solubility in various solvents, gel electrophoresis, and immunological techniques. The finding explains the wide distribution of allergens in various seeds.

Journal Article↗

Isolation of a cDNA Clone for alpha-Amylase in Mung Bean Cotyledons : Analysis of alpha-Amylase mRNA Levels in Cotyledons during and following Germination of Mung Bean Seeds.

A cDNA was isolated that codes for alpha-amylase in mung bean (Vigna radiata) cotyledons, and the nucleotide sequence was determined. The deduced amino acid sequence (421 amino acid residues) is about 65% homologous with those of barley alpha-amylases. By comparing the deduced sequence with the sequence of the purified alpha-amylase, it was inferred that 23 N-terminal amino acids of a nascent polypeptide represent a signal peptide. Northern blot analysis showed that the levels of alpha-amylase mRNA are in parallel with the activities of alpha-amylase synthesis in cotyledons. Under the conditions where the solute leakage from cotyledons is accelerated during imbibition, a rapid increase in the amount of the alpha-amylase mRNA occurs. We postulate that a factor(s) which regulates in an inhibitory manner the alpha-amylase expression at the transcriptional level may be present in dry cotyledons and be removed by leakage.

Journal Article↗