• Food Science of Animal Resources
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• v.35 no.2
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• pp.265-271
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• 2015

In a previous study, hydrolysates of porcine placenta were obtained and the extraction efficiency for proteins and amino acids was compared between sub- and super-critical water extraction systems; optimum efficiency was found to be achieved using subcritical water ($170^{\circ}C$, 10 bar). In this study, the effects of adding ethanol to the subcritical water system were investigated. The lowest-molecular-weight extraction product detected weighed 434 Da, and the efficiency of extraction for low-molecular-weight products was increased when either the concentration of ethanol was decreased, or the extraction time was lengthened from 10 min to 30 min. The highest concentration of free amino acids (approximately 8 mM) was observed following 30 min extraction using pure distilled water. The concentration of free amino acids was significantly lower when ethanol was added or a shorter extraction time was used (p<0.05). Color change of the solution following extraction was measured. There were no significant differences in color between lysates produced with different extraction times when using distilled water (p>0.05); however, using different extraction times produced significant differences in color when using 20% or 50% ethanol solution for subcritical extraction (p<0.05). The range of pH for the hydrolysate solutions was 6.4-7.5. In conclusion, the investigated extraction system was successful in the extraction of $\leq$ 500 Da hydrolysates from porcine placenta, but addition of ethanol did not yield higher production of low-molecular-weight hydrolysates than that achieved by DW alone.

• 한국생물공학회:학술대회논문집
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• 2003.10a
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• pp.696-696
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• 2003

• Korean Journal Plant Pathology
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• v.11 no.4
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• pp.318-323
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• 1995

The effect of AF-toxin I produced by the strawberry pathotype of Alternaria alternata on the protein synthesis of susceptible strawberry protoplasts was examined by using the radiolabeled amino acids. The incorporation of the radiolabeled amino acids into newly synthesized proteins in the strawberry protoplasts was stimulated by the toxin treatment at relatively low concentrations (2.2$\times$10-11 to 2.2$\times$10-9 M), but not at higher concentrations (2.2$\times$10-8 to 2.2$\times$10-6 M). An one-dimensional SDS-polyacrylamide gel electrophoresis revealed no detectable differences in the proteins synthesized in both the toxintreated and untreated protoplasts. The susceptible strawberry protoplasts were treated with AF-toxin I and stained with Fluostain I to detect the extracellular polysaccharides. The toxin treatment induced the accumulation of extracellular polysccharides in a dose-dependent manner. These results indicate a transient activation of cellular metabolism in the susceptible cells by the toxin exposure.

• Journal of Nutrition and Health
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• v.10 no.2
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• pp.27-34
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• 1977

The present study was carried out to evaluate the nutritional quality of rabbit meat protein. The composition of amino acids contained in rabbit meat was compared with those of other animal meats such as beef, pork and chicken. Also included in this study was the question whether the cooking and storage conditions affect the amino acid composition and the pepsindigestibility of rabbit meat protein. The results are summarized as follows: 1. The large variation observed from sample to sample of EAA (essential amino acid) composition in rabbit meat was found to be an interesting but peculiar property of rabbit meat protein. The most limiting amino acid of rabbit meat protein was phenylalanine, whereas methionine was the first limiting amino acid of both beef and pork proteins. Chemical scores of various meat proteins were 68, 65, 66, and 74 for rabbit meat, beef, pork, and chicken respectively. 2. In pan roasting, the EAA damaged most by heat was methionine (15%). When cooked after two months of frozen storage, lysine decreased most. 3. Higher pepsin digestibility was obtained by cooking rabbit meat after seasoned in alcohol, ginger juice, and other spices compared with various other cooking conditions without seasoning. The pepsin digestibility value was even higher for the seasoned meat than for the raw meat. 4. Among various meats tested the rabbit meat showed the lowest pepsin digestibility. 5. A simple measurement of released methionine could be used to determine relative digestibility instead of measuring $NH_2-N$ content after pepsin digestion. From all the results obtained in this study it can be concluded that rabbit meat is a good Protein food item when used fresh and stored properly to prevent rancidity problems. It is suggested to study further the peroxidation effect of unsaturated fatty acids on protein quality. This study was supported by the Ministry of Science and Technology in Korea.

• Korean journal of food and cookery science
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• v.8 no.4
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• pp.379-385
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• 1992

1. Amino acid compositions were determined by amino acid analyzer. Through the analysis of these samples, it was found that glutamic acid was the most abundant; glycine, aspartic acid, lysine and threonine were rich; and tryptophan and methionine were the limiting amino acid. 2. Albumins, globulins, gliadins and glutelins were extracted from the Kangwon hull, Kangwon rice buckwheat, and wheat. The relative proportions of protein fractions were 52.45 : 10.14 : 16.61 : 20.80% in Kangwon hull buckwheat, 21.10 : 13.80 : 28.40 : 36.70% in Kangwon rice buckwheat and 6.87 : 1.65 : 42.85 : 48.6% in wheat, in the order of albumins, globulins, gliadins and glutelins. 3. Polyacrylamide gel electrophoresis (PAGE) and SDS-polyacrylamide gel electrophoresis (SDS-PAGE) were performed to identify the subfractions of each protein fraction. The electrophoregrams of PAGE showed that the same fractions of both Kangwon hull buckwheat protein and Kangwon rice buckwheat protein had very similar electrophoretic patterns to each other respectively, but there were significant differences in the patterns between buckwheat proteins and wheat proteins.

• Molecules and Cells
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• v.27 no.6
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• pp.629-634
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• 2009

G protein-coupled receptors (GPCRs) are part of multi-protein networks called 'receptosomes'. These GPCR interacting proteins (GIPs) in the receptosomes control the targeting, trafficking and signaling of GPCRs. PDZ domain proteins constitute the largest protein family among the GIPs, and the predominant function of the PDZ domain proteins is to assemble signaling pathway components into close proximity by recognition of the last four C-terminal amino acids of GPCRs. We present here a machine learning based approach for the identification of GPCR-binding PDZ domain proteins. In order to characterize the network of interactions between amino acid residues that contribute to the stability of the PDZ domain-ligand complex and to encode the complex into a feature vector, amino acid contact matrices and physicochemical distance matrix were constructed and adopted. This novel machine learning based method displayed high performance for the identification of PDZ domain-ligand interactions and allowed the identification of novel GPCR-PDZ domain protein interactions.

• The Plant Pathology Journal
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• v.23 no.4
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• pp.281-286
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• 2007

Interactions between viral proteins and host proteins are essential for virus replication. Especially, translation of viral genes completely depends on the host machinery. In potyviruses, interactions of genome-linked viral protein (VPg) with host translation factors including eIF4E, eIF(iso)4E, and poly(A)-binding protein (PABP) has previously been characterized. In this study, we investigated interactions between Soybean mosaic virus (SMV) viral proteins and host translation factors by yeast two-hybrid system. SMV VPg interacted with eIF4E, eIF(iso)4E, and PABP in yeast two-hybrid system, while SMV helper component proteinase (HC-pro) interacted with neither of those proteins. The interaction between SMV NIb and PABP was also detected. These results are consistent with those reported previously in other potyviruses. Interestingly, we found reproducible and specific interactions between SMV coat protein (CP) and PABP. Deletion analysis showed that the region of CP comprising amino acids 116 to 206 and the region of PABP comprising amino acids 520 to 580 are involved in CP/PABP interactions. Soybean library screening with SMV NIb by yeast two-hybrid assay also identified several soybean proteins including chlorophyll a/b binding preprotein, photo-system I-N subunit, ribulose 1,5-biphosphate carboxylase, ST-LSI protein, translation initiation factor 1, TIR-NBS type R protein, RNA binding protein, ubiquitin, and LRR protein kinase. Altogether, these results suggest that potyviral replicase may comprise a multi-protein complex with PABP, CP, and other host factors.

• Korean Journal Plant Pathology
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• v.14 no.3
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• pp.240-246
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• 1998

A cDNA encoding desiccation-related protein was isolated from a flower bud cDNA library of Chinese cabbage (C-DH) and its nucleotide sequence was characterized. It contains 679 bp nucleotides with 501 bp open reading frame. The amino acid sequence of the putative protein showed the highest amino acid sequence homology (79 % identity) to dehydrin protein in Gossypium hirsutum. Also, the C-DH shares 48-52% amino acid sequence identity with the other typical dehydrin proteins in plant cells. When the amino acid sequence of their proteins were aligned, several peptide motifs were well conserved, of which function has to be solved. Particularly the C-DH contains 15 additional amino acids at its N-terminus. Genomic Southern blot analysis using the coding region of C-DH showed that the C-DH consists of a single copy gene in Chinese cabbage genome. The C-DH mRNA, whose transcript size is 0.7 kb, was expressed with a tissue-specific manner. It was highly expressed in seed, flower buds and low expression as detected in root, stem or leaf tissues of Chinese cabbage. And the transcript level of C-DH was significantly induced by the treatment of plant hormone, abscisic acid and water-deficit conditions.

• Plant Resources
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• v.1 no.2
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• pp.92-97
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• 1998

An isolate of barley yellow mosaic virus(BaYMV-HN) obtained from Haenam, Korea was compared with two BaYMV strains. BaYMV-Ⅱ-1 from Japan and BaYMV-G from Germany. The sequence of the 3'-terminal 3817nucleotides[excluding the poly (A) tail] of RNA 1 of BaYMV-HN was determined to start within a long open reading frame coding for a part of the NIa-VPg polymerase(26 amino acids). NIa-Pro polymerase (343 amino acids), NIb polymerase(528 amino acids) and the entire capsid protein(297 amino acids), which is followed by a noncoding region(NCR) of 235 nucelotides. In the partial ORFs, BaYMV-HN shows higher sequence homology with BaYMV-Ⅱ-1(99.5%) than BaYMV-G(92.7%). The 3' non-coding regions of BaYMV-HN(235nt) shows higher nucleotide sequence homology with BaYMV-G(235nt)(99.6%) than BaYMV-Ⅱ-1(231nt)(97.0%). The 3' NIa-Pro protein sequence of BaYMV-HN shows higher amino acid sequence homology with BaYMV-Ⅱ-1(95.0%) than BaYMV-G(93.6%), but, NIb protein sequence of BaYMV-HN shows same all amino acid sequence. The capsid protein sequence of BaYMV-HN(297aa) shows same with BaYMV-Ⅱ-1, and shows higher nucleotide sequence homology with BaYMV-UK (from United Kingdom)(97.3%) than BaYMV-G(96.9%) and G2(96.9%). Difference of capsid protein amino acid were 0-9 between the Japan, United Kingdom and Germany and were 2-6 between all Korean isolates. Many of the amino acid differences are located in the N-terminal regions of the capsid proteins from 1 to 74 amino acid positions.

• Proceedings of the Korean Society of Crop Science Conference
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• 2017.06a
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• pp.86-86
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• 2017

Prolamins are the main seed storage proteins in cereals. Gluten proteins seem to be prolamins because their primary structure have the meaningful quantity of proline and glutamine amino acid residues. Gluten proteins are found in crops such as wheat (Triticum aestivum), barley (Hordeum vulgare), and rye (Secale cereale) which are major food crops in the Triticeae tribe. Glutenin and gliadin, hordein, and secalin are typical gluten proteins found in wheat, barley, and rye, respectively. Gluten affect grain quality so that many researches, such as isolation or characterization of their genes, have been carried out. To improve the quality of grains in the Triticeae tribe, it is necessary to understand the relationship within their gluten proteins and their evolutionary changes. The sequences of nucleotides and amino acids of gluten protein including glutenins, gliadins, hordeins, and secalins were retrieved from NCBI (https://www.ncbi.nlm.nih.gov/) and Uniprot (http://www.uniprot.org/). The sequence analysis and the phylogenetic analysis of gluten proteins were performed with various website tools. The results demonstrated that gluten proteins were grouped with their homology and were mostly corresponded with the previous reports. However, some genes were moved, duplicated, or disappeared as evolutionary process. The obtained data will encourage the breeding programs of wheat, barley, rye, and other crops in the Triticeae tribe.