Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:A7KAX9 (grit)
 1,275 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The amino acids composition of summary proteins in unground buckwheat of four common and promising varieties grown in the Ukraine was investigated by using ion-exchange chromatography with an automatic analyzor Hd-1200 E. Between individual varieties of buckweheat no essential differences in the amino acids content were in evidence. The total proteins of the buckwheat grit contain high quantities of lysine, treonine, leucine, glutamic acid and arginine. The amino acids score was instrumental in determining the biological value and in eliciting amino acids limiting this value in different grits. These data may be made use of in the practice of public catering for estimating formulae of meals prepared with grits differently combined with other products securing an improved amino acids composition of ready-to-eat meals.
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PMID:[Amino acid composition and biologic value of the proteins of several sorts of buckwheat]. 96 74

Potential use of the high protein by-product of beer production from 77% sorghum malt and 23% maize grit was investigated. Red sorghum spent grains (RSSG) and white sorghum spent grains (WSSG) contained 23.4 and 19.3% crude protein (CP), 54 and 43% dietary fiber (NDF), 1.44 and 0.78% ash, 4.5 and 3.2% hexane extract and tannin content of 7.5 and 1.0 mg/g catechin equivalent respectively. Magnesium was the most abundant mineral in both RSSG and WSSG--185 and 140 mg/kg, respectively. Calcium, zinc, iron and copper were generally low. Both samples contained cadmium 1.12 (WSSG), 1.19 (RSSG) and lead at 1.38 mg/kg. Lysine was the limiting amino acid (chemical score 0.55) in both samples. Other essential amino acids were adequate or surplus. Stearic acid was the predominant fatty acid with varying levels of lauric, myristic, palmitic, and oleic acids in both samples. Feed intake and weight gain were highest in rats fed 26.3% WSSG (contributing 50% of the diet protein) but protein efficiency ratio (PER) and net protein retention (NPR) were highest in diets where spent grains contributed just 25% of the diet protein. True digestibility of diets decreased as dietary fiber content increased such that animals on diets containing 100% spent grain protein (above 20% NDF) lost weight.
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PMID:Nutritional evaluation of spent grains from sorghum malts and maize grit. 797 86

Osteoblasts exhibit a more differentiated morphology on surfaces with rough microtopographies. Surface effects are often mediated through integrins that bind the RGD motif in cell attachment proteins. Here, we tested the hypothesis that modulating access to RGD binding sites can modify the response of osteoblasts to surface microtopography. MG63 immature osteoblast-like cells were cultured on smooth (Ti sputter-coated Si wafers) and rough (grit blasted/acid etched) Ti surfaces that were modified with adsorbed monomolecular layers of a comb-like graft copolymer, poly-(L-lysine)-g-poly(ethylene glycol) (PLL-g-PEG), to limit nonspecific protein adsorption. PLL-g-PEG coatings were functionalized with varying amounts of an integrin-receptor-binding RGD peptide GCRGYGRGDSPG (PLL-g-PEG/PEG-RGD) or a nonbinding RDG control sequence GCRGYGRDGSPG (PLL-g-PEG/PEG-RDG). Response to PLL-g-PEG alone was compared with response to surfaces on which 2-18% of the polymer sidechains were functionalized with the RGD peptide or the RDG peptide. To examine RGD dose-response, peptide surface concentration was varied between 0 and 6.4 pmol/cm(2). In addition, cells were cultured on uncoated Ti or Ti coated with PLL-g-PEG or PLL-g-PEG/PEG-RGD at an RGD surface concentration of 0.7 pmol/cm(2), and free RGDS was added to the media to block integrin binding. Analyses were performed 24 h after cultures had achieved confluence on the tissue culture plastic surface. Cell number was reduced on smooth Ti compared to plastic or glass and further decreased on surfaces coated with PLL-g-PEG or PLL-g-PEG/PEG-RDG, but was restored to control levels when PLL-g-PEG/PEG-RGD was present. Alkaline phosphatase specific activity and osteocalcin levels were increased on PLL-g-PEG alone or PLL-g-PEG/PEG-RDG, but PLL-g-PEG/PEG-RGD reduced the parameters to control levels. On rough Ti surfaces, cell number was reduced to a greater extent than on smooth Ti. PLL-g-PEG coatings reduced alkaline phosphatase and increased osteocalcin in a manner that was synergistic with surface roughness. The RDG peptide did not alter the PLL-g-PEG effect but the RGD peptide restored these markers to their control levels. PLL-g-PEG coatings also increased TGF-beta1 and PGE(2) in conditioned media of cells cultured on smooth or rough Ti; there was a 20x increase on rough Ti coated with PLL-g-PEG. PLL-g-PEG effects were inhibited dose dependently by addition of the RGD peptide to the surface. Free RGDS did not decrease the effect elicited by PLL-g-PEG surfaces. These unexpected results suggest that PLL-g-PEG may have osteogenic properties, perhaps correlated with effects that alter cell attachment and spreading, and promote a more differentiated morphology.
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PMID:RGD-containing peptide GCRGYGRGDSPG reduces enhancement of osteoblast differentiation by poly(L-lysine)-graft-poly(ethylene glycol)-coated titanium surfaces. 1476 25

Trefoil factors are essential healing initiators participating in mucosal reconstitution and tissue morphogenesis, especially on the surfaces of the gastrointestinal tract. This family has been cloned and characterized predominantly from mammals and amphibians. Avian species ingest stone and grit to help digest food, which may expose their gut to severe physical conditions. To further the understanding of the function of the TFF gene family across species, we undertook this research to clone, sequence, and characterize the spatio-temporal expression patterns of chicken TFF2 (ChTFF2) cDNA. Bioinformatics analysis of the promoter region and deduced amino acid sequence demonstrated that ChTFF2 contained unique characteristics; specifically the chicken promoter has multiple start sites and the protein contains a series of Lys-Lys-Val repeats. Unlike mammals, where TFF2 is detected primarily in the stomach, and occasionally in the proximal duodenum, chicken TFF2 transcripts are found throughout the gastrointestinal tract, with major expression sites in the glandular and muscular stomach as well as evident expression in the colon, small intestine, cecal tonsil and crop. Temporal analysis of intestinal ChTFF2 transcripts by quantitative RT-PCR showed high levels in embryos and a trend of constant expression during embryonic and post-hatch development, with a reduction occurring around hatch. Phylogenetic analysis highlighted the conservation of TFF proteins and functional divergence of trefoil domains, which suggest a transitional role in the bird during evolution.
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PMID:Evolution of trefoil factor(s): genetic and spatio-temporal expression of trefoil factor 2 in the chicken (Gallus gallus domesticus). 2182 80