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Remaining Proteins (remaining + protein)

Distribution by Scientific Domains

Life Sciences	50%

Selected Abstracts

RECOVERY OF SINAPIC ACID FROM A WASTE STREAM IN THE PROCESSING OF YELLOW MUSTARD PROTEIN ISOLATE

JOURNAL OF FOOD PROCESS ENGINEERING, Issue 2 2008
N. PRAPAKORNWIRIYA
ABSTRACT A large amount of waste permeates generated from the processing of yellow mustard protein was concentrated fivefold using a nanofilter with a molecular weight cut off of 1,000 Da, while approximately 74% of sinapic acid was retained. Sinapic acid was then released from sinapine, its esterified form, by an alkaline hydrolysis. The hydrolyzed solution was acidified to prevent oxidation of the sinapic acid and to precipitate the remaining proteins. Subsequently, sinapic acid and other phenolics were extracted by a two-stage extraction using a mixture of diethyl ether and ethyl acetate (1:1), 165-min extraction time and permeate-to-solvent ratio of 1:2. Approximately 95% of the sinapic acid in the acidified permeate was finally concentrated in the solvent phase. PRACTICAL APPLICATIONS This development has led to an economical process to recover phenolics and to treat effluent from a process of oilseed protein while reducing the use of water during the extraction of protein. A reduction of water usage makes the processing of oilseed protein isolate more economically attractive, and the recovered phenolics may find a use as a nutraceutical. The developed process is not only limited to the recovery of phenolics from mustard, but also applied for recovering phenolic acids, specifically sinapic acid, from waste water from membrane processing of protein from mustard and similar polyphenol-containing oilseeds. [source]

Tag-mediated fractionation of yeast ribosome populations proves the monomeric organization of the eukaryotic ribosomal stalk structure

MOLECULAR MICROBIOLOGY, Issue 2 2003
Esther Guarinos
Summary The analysis of the not well understood composition of the stalk, a key ribosomal structure, in eukaryotes having multiple 12 kDa P1/P2 acidic protein components has been approached using these proteins tagged with a histidine tail at the C-terminus. Tagged Saccharomyces cerevisiae ribosomes, which contain two P1 proteins (P1, and P1,) and two P2 proteins (P2, and P2,), were fractionated by affinity chromatography and their stalk composition was determined. Different yeast strains expressing one or two tagged proteins and containing either a complete or a defective stalk were used. No indication of protein dimers was found in the tested strains. The results are only compatible with a stalk structure containing a single copy of each one of the four 12 kDa proteins per ribosome. Ribosomes having an incomplete stalk are found in wild-type cells. When one of the four proteins is missing, the ribosomes do not carry the three remaining proteins simultaneously, containing only two of them distributed in pairs made of one P1 and one P2. Ribosomes can carry two, one or no acidic protein pairs. The P1,/P2, and P1,/P2, pairs are preferentially found in the ribosome, but they are not essential either for stalk assembly or function. [source]

The Arabidopsis thaliana ATP-binding cassette proteins: an emerging superfamily

PLANT CELL & ENVIRONMENT, Issue 5 2000
T. G. E. Davies
ABSTRACT Solute transport systems are one of the major ways in which organisms interact with their environment. Typically, transport is catalysed by integral membrane proteins, of which one of the largest groups is the ATP-binding cassette (ABC) proteins. On the basis of sequence similarities, a large family of ABC proteins has been identified in Arabidopsis. A total of 60 open reading frames (ORFs) encoding ABC proteins were identified by BLAST homology searching of the nuclear genome. These 60 putative proteins include 89 ABC domains. Based on the assignment of transmembrane domains (TMDs), at least 49 of the 60 proteins identified are ABC transporters. Of these 49 proteins, 28 are full-length ABC transporters (eight of which have been described previously), and 21 are uncharacterized half-transporters. Three of the remaining proteins identified appear to be soluble, lacking identifiable TMDs, and most likely have non-transport functions. The eight other ORFs have homology to the nucleotide-binding and transmembrane components of multi-subunit permeases. The majority of ABC proteins found in Arabidopsis can, on the basis of sequence homology, be assigned to subfamilies equivalent to those found in the yeast genome. This assignment of the Arabidopsis ABC proteins into easily recognizable subfamilies (with distinguishable subclusters) is an important first step in the elucidation of their functional role in higher plants. [source]

In search for correlation among markers for limbal stem cells niche

ACTA OPHTHALMOLOGICA, Issue 2009
C CURCIO
Purpose The corneoscleral limbus is known to be the site of corneal epithelial stem cells (SC). Several molecules have been proposed as SC markers but none of them is able to univocally identify them. The aim of this study was to evaluate co-expression of different SC markers in human limbus. Methods In this work five corneoscleral specimens from normal human donor eye-bank eyes (age 52-73 years) were fixed in formalin, divided in 8 segments, embedded in paraffin and examined by immunohistochemistry and immunofluorescence for p63, vimentin (vim), laminin 5, integrin (Int) ,6, Int ,1, Int ,4, connexin 43, ki67 and N-cadherin positivity. We firstly analyzed the distribution and the anatomical structure of limbal crypts in each of the segments. Then we evaluated the percentage of positive areas in the niches. Finally we looked for colocalizations and possible correlations among markers. Results We confirmed a different number of niches among the segments of the same corneoscleral rim. Moreover we observed high variability of niches number among patients which interestingly correlates with the percentage of p63 positivity of niche cells. Confocal microscopy double staining for p63 and vim did not show evident colocalization and vim + cells were seen in the superficial layers rather than in the deep layer of crypts. Int ,1 staining directly correlated with p63 positivity while the remaining proteins appeared variably and widely distributed Conclusion Colocalization was evident at least for two SC markers (Int ,1/p63) within the basal layers, while vim, expressed mainly in the superficial layers could act as late progenitor cell marker. [source]