• Title/Summary/Keyword: proteins and amino acids

Search Result 597, Processing Time 0.029 seconds

Varietal Difference of Protein Content and Amino Acid Composition in Peanuts (땅콩품종의 단백질 함량과 아미노산 조성)

  • Lee, Jung-Il;Park, Hee-Woon;Kang, Kwang-Hee;Kim, Ki-Joon
    • KOREAN JOURNAL OF CROP SCIENCE
    • /
    • v.35 no.5
    • /
    • pp.424-439
    • /
    • 1990
  • The protein content of seed meal were examined to evaluate genotypes of higher protein content from 164 peanut germplasms. The variations in amino acids content were investigated from nine Korean leading varieties grown at five locations. Amino acids contents of protein fractions were also ana lysed in the present study, too. The results of the study were summarized as fallows. The seed protein of 164 peanut varieties averaged 24.5% ranging from 19.5% to 28.7%, showed 9.2% varietal variation in proteins. Differences were not observed in protein content between plant types, however, protein contents were higher in small-seeded than large seeded varieties. The differences were more greater particulaly in Spanish type varieties. The varieties introduced from Taiwan and Philippine showed higher protein contents, and the cultivars or lines bred in Korea and introduced from Japan were lower in protein contents. protein contents showed non-significantly negative correlations with 100-kernel weight and pod weight per plant, but positive correlations were observed between oil and protein content in all types of peanuts. Significant differences among the varieties and locations were observed for total, essential and non-essential amino acids contents, and aspartic acid. Locational differences for arginine, lysine, methionine, threonine, glutamic acid, glycine and tyrosine, and varietal difference for phenylalanene were revealed as significant. The limiting amino acids from the leading varieties were isoleucine, methionine, threonine, alanine and tyrosine, comparing with FAO recommanding levels of amino acids. Among the protein fractions prolamins was the highest in total amino acids, but essential amino acids was the highest in globulins

  • PDF

Nucleotide Sequence of 7.2 kb Mitochondrial Linear Plasmid DNA in Pleurotus ostreatus (Pleurotus ostreatus 미토콘드리아의 7.2 kb 선상 플라스미드 염기서열 분석)

  • 윤혜숙;구용범;노정혜
    • Korean Journal of Microbiology
    • /
    • v.37 no.1
    • /
    • pp.37-41
    • /
    • 2001
  • Two linear plasmid-like DNAs, 10.2 kb and 7.2 kb were found in the mitochondria of P. ostreatus. They have covalently linked 5'-terminal proteins in both ends. Two continuous fragments of 4.7 kb and 2.3 kb from 7.2 kb DNA were cloned and sequenced. Two long open reading frames (ORF1; 2982 bp, 993 a.a and ORF2; 2703 bp, 900 a.a) and one short open reading frame(ORF3; 771 bp, 256 a.a) were found in the 7.2 kb plasmid. The putative ORF1 and ORF2 have conserved motifs of DNA polymerases and RNA polymerases, respectively, while the ORF3 has homologous regions with phosphatase from Plasmodium, and also with adhesine from Mycoplasma.

  • PDF

국립공원 북한산의 환경평가에 관하여 - 도봉산지역 일대를 중심으로-

  • 박봉규
    • Proceedings of the Botanical Society of Korea Conference
    • /
    • 1985.08b
    • /
    • pp.35-48
    • /
    • 1985
  • Plastids, which are organelles unique to plant cells, bear their own genome that is organized into DNA-protein complexes (nucleoids). Regulation of gene expression in the plastid has been extensively investigated because this organelle plays an important role in photosynthesis. Few attempts, however, have been made to characterize the regulation of plastid gene expression at the chromosomal structure, using plastid nucleoids. In this report, we summarize the recent progress in the characterization of DNA-binding proteins in plastids, with special emphasis on CND41, a DNA binding protein, which we recently identified in the choloroplast nucleoids from photomixotrophically cultured tobacco cells. CND41 is a protein of 502 amino acids which consisted of a transit peptide of 120 amino acids and a mature protein of 382 amino acids. The N-terminal of the 'mature' protein has lysine-rich region which is essential for DNA-binding. CNA41 also showed significant identities to some aspartyl proteases. Protease activity of purified CND41 has been recently confirmed and characterized. On the other hand, characterization of accumulation of CND41 both in wild type and transgenic tobacco with reduced amount of CND41 suggests that CND41 is a negative regulator in chloroplast gene expression. Further investigation indicated that gene expression of CND41 is cell-specifically and developmentally regulated as well as sugar-induced expression. The reduction of CND41 expression in transgenic tobacco also brought the stunted plant growth due to the reduced cell length in stem. GA3 treatment on apical meristem reversed the dwarf phenotype in the transformants. Effects of CND41 expression on GA biosynthesis will be discussed

  • PDF

In Vitro Combinatorial Mutagenesis of the 65th and 222nd Positions of the Green Fluorescent Protein of Aequarea victoria

  • Nakano, Hideo;Okumura, Reiko;Goto, Chinatsu;Yamane, Tsuneo
    • Biotechnology and Bioprocess Engineering:BBE
    • /
    • v.7 no.5
    • /
    • pp.311-315
    • /
    • 2002
  • By the in vitro combinatorial mutagenesis, which is a sequential reaction of PCR mutagenesis and in vitro coupled transcription/translation with Escherichia coli S30 extract, S65 and E222 of green fluorescent protein of Aequarea victoria were comprehensively changed to all possible combinations of amino acids, thus totally 400 mutant (including a wild type) proteins were simultaneously produced and their fluorescent properties were analyzed. Although a few mutations had been reported so far at the 222nd position, replacement E222 to all other19 amino acids gave fluorescent signal to the mutants by changing Ser 65 to Ala together. Among the mutants, replacement to G, A, S, Q, H and C gave relatively high fluorescence. The in vitro combinatorial mutagenesis, therefore, has been proved valuable for comprehensive structure-function studies of proteins.

A New-Generation Fluorescent-Based Metal Sensor - iLOV Protein

  • Ravikumar, Yuvaraj;Nadarajan, Saravanan Prabhu;Lee, Chong-Soon;Rhee, Jin-Kyu;Yun, Hyungdon
    • Journal of Microbiology and Biotechnology
    • /
    • v.25 no.4
    • /
    • pp.503-510
    • /
    • 2015
  • The iLOV protein belongs to a family of blue-light photoreceptor proteins containing a light-oxygen-voltage sensing domain with a noncovalently bound flavin mononucleotide (FMN) as its chromophore. Owing to advantages such as its small size, oxygen-independent nature, and pH stability, iLOV is an ideal candidate over other reporter fluorescent proteins such as GFP and DsRed. Here, for the first time, we describe the feasibility of applying LOV domain-based fluorescent iLOV as a metal sensor by measuring the fluorescence quenching of a protein with respect to the concentration of metal ions. In the present study, we demonstrated the inherent copper sensing property of the iLOV protein and identified the possible amino acids responsible for metal binding. The fluorescence quenching upon exposure to Cu2+ was highly sensitive and exhibited reversibility upon the addition of the metal chelator EDTA. The copper binding constant was found to be 4.72 ± 0.84 µM. In addition, Cu2+-bound iLOV showed high fluorescence quenching at near physiological pH. Further computational analysis yielded a better insight into understanding the possible amino acids responsible for Cu2+ binding with the iLOV protein.

Identification of a Protein Interacting with Human Nebulin SH3 Domain by Yeast Two-hybrid Screening

  • Lee, Min-A;Kim, Ji-Hee;Min, Byung-In;Park, Soo-Ho;Ko, Han-Suk;Kim, Chong-Rak
    • Biomedical Science Letters
    • /
    • v.7 no.2
    • /
    • pp.59-64
    • /
    • 2001
  • Nebulin is an unusually large actin-binding protein specific to the skeletal muscle of vertebrates. The correlation of nebulin size with thin filament length have led to the suggestion that nebulin acts as a molecular ruler for the length of thin filaments. An SH3 domain occupies the C terminus of nebulin, in the sarcomeric Z-disk and is preceded by a 120-residue stretch containing multiple putative phosphorylation sites. SH3 domain mediates protein-protein interaction involved in the subcellular localization of proteins, cytoskeletal organization and signal transduction. However the binding partner and physiological role of nebulin SH3 domains remains unknown. Using the yeast two-hybrid system, we identified supervillin, an actin-binding protein, as a nebulin SH3 domain-interacting protein. The SH3 domain of nebulin binds to the sequence encoding amino acids 977 to 1335 of supervillin. But the sequence encoding amino acids 977 to 1335 displays weaker binding than the sequence encoding amino acids 977 to 1788.

  • PDF

The Effect of Irradiation on Meat Products

  • Yea-Ji Kim;Ji Yoon Cha;Tae-Kyung Kim;Jae Hoon Lee;Samooel Jung;Yun-Sang Choi
    • Food Science of Animal Resources
    • /
    • v.44 no.4
    • /
    • pp.779-789
    • /
    • 2024
  • The effects of irradiation on meat constituents including water, proteins, and lipids are multifaceted. Irradiation leads to the decomposition of water molecules, resulting in the formation of free radicals that can have both positive and negative effects on meat quality and storage. Although irradiation reduces the number of microorganisms and extends the shelf life of meat by damaging microbial DNA and cell membranes, it can also accelerate the oxidation of lipids and proteins, particularly sulfur-containing amino acids and unsaturated fatty acids. With regard to proteins, irradiation affects both myofibrillar and sarcoplasmic proteins. Myofibrillar proteins, such as actin and myosin, can undergo depolymerization and fragmentation, thereby altering protein solubility and structure. Sarcoplasmic proteins, including myoglobin, undergo structural changes that can alter meat color. Collagen, which is crucial for meat toughness, can undergo an increase in solubility owing to irradiation-induced degradation. The lipid content and composition are also influenced by irradiation, with unsaturated fatty acids being particularly vulnerable to oxidation. This process can lead to changes in the lipid quality and the production of off-odors. However, the effects of irradiation on lipid oxidation may vary depending on factors such as irradiation dose and packaging method. In summary, while irradiation can have beneficial effects, such as microbial reduction and shelf-life extension, it can also lead to changes in meat properties that need to be carefully managed to maintain quality and consumer acceptability.

Purification and Characterization of a 25 kDa Cathepsin L-like Protease from the Hemocyte of Coleopteran Insect, Tenebrio molitor Larvae

  • Jang, Kyung-Suk;Cho, Mi-Young;Choi, Hye-Won;Lee, Kang-Moon;Kim, Mi-Hee;Lee, Young-Un;Kurata, Shoichiro;Natori, Shunji;Lee, Bok-Luel
    • BMB Reports
    • /
    • v.31 no.4
    • /
    • pp.364-369
    • /
    • 1998
  • Insect plasma protein is abundant in the hemolymph of holometabolous insect larvae and is used as a source of amino acids and energy for construction of adult structures during metamorphosis. In order to understand the mechanism of decomposition of larval plasma proteins by hemocyte protease, we tried to purify a cysteine protease from the hemocyte lysate by using Carbobenzoxy-L-Phenylalanyl-L-Arginine-4-Methyl-Coumaryl-7-Amide (Z-Phe-Arg-MCA) as substrate and to identify plasma proteins that are selectively susceptible to the purified protease. Here, we describe the purification and characterization of a cysteine protease that specifically hydrolyzes the plasma protein of the coleopteran insect, Tenebrio molitor, larvae. The molecular mass of this enzyme was 25 kDa, as determined by SDS-PAGE under reducing conditions. The amino acids sequence of its $NH_{2}-terminus$ was determined to be Leu-Pro-Gly-Gln-Ile-Asp-Trp-Arg-Asp-Lys-Gly. This sequence contained Pro, Asp, and Arg residues, conserved in many papain superfamily enzymes. The specific cysteine protease inhibitors, such as E-64 and leupetin, inhibited its hydrolytic activity. One plasma protein with a molecular mass of 48 kDa was selectively hydrolyzed within 3 h when the purified enzyme and plasma proteins were incubated in vitro. However, the 48 kDa protein was not hydrolyzed by the purified 25 kDa protease in the presence of E-64. Western blotting analysis at various developmental stages showed that the purified enzyme was detected at larvae, pupae, and adult stages, but not the embryo stage.

  • PDF

Study on the Chemical Composition in Bamboo Shoot, Lotus Root and Burdock - Free Sugar, Fatty Acid, Amino Acid and Dietary Fiber Contents - (죽순, 연근, 우엉의 성분분석 - 유리당, 지방산, 아미노산 및 식이섬유의 조성 -)

  • 한수정;구성자
    • Korean journal of food and cookery science
    • /
    • v.9 no.2
    • /
    • pp.82-87
    • /
    • 1993
  • This experiment was carried out to determine the total dietary fiber content and free sugar, fatty acid, amino acid compositions in bamboo shoot, lotus root and burdock. Bamboo shoot contained 3.05% of proteins, 0.48% of lipids, 2.45% of fibers, which were larger than those of other samples (lotus root and burdock). Burdock contained more sugars than the others as 18.64%. On a dry matter basis, total dietary fiber by Prosky AOAC method were 62.5% for bamboo shoot, 17.9% for lotus root and 41.9% for burdock. Therefore, the content of dietary fiber in bamboo shoot was the most abundant among them. Free sugar contents (glucose, fructose and sucrose) of the sample were analyzed by HPLC. Sucrose was the most abundant in both bamboo shoot and lotus root, and the content of fructose and sucrose in burdock were almost same. The major fatty acids in bamboo shoot, lotus root and burdock analyzed by GC were palmitic and linoleic acid. Also, linolenic acid were abundent only in bamboo shoot. The results of amino acid analysis showed that aspartic acid, glutamic acid and Iysine were the most abundent amino acids in the sample. Bamboo shoot contained large percentage of protein, the sweet-tasting amino acids and lipid than the other samples. Therefore bamboo shoot can be used as a flavor material because they contain plenty of the sweet-lasting amino acid and free sugar. Bamboo shoot and burdock can be used as potential source of dietary fiber because of the high content of dietary fiber in those samples.

  • PDF

Evaluation of Three Plant Proteins for Fish Meal Replacement in Diet for Growing Olive Flounder Paralichthys olivaceus (육성기 넙치(Paralichthys olivaceus) 사료 내 어분 대체를 위한 식물성 원료 평가)

  • Lim, Hyunwoon;Kim, Min-Gi;Shin, Jaehyeong;Shin, Jaebeom;Hur, Sang-Woo;Lee, Bong-Joo;Lee, Kyeong-Jun
    • Korean Journal of Fisheries and Aquatic Sciences
    • /
    • v.53 no.3
    • /
    • pp.464-470
    • /
    • 2020
  • This study was conducted to replace fish meal (FM) with three plant proteins (soybean meal, soy protein concentrate, and wheat gluten) in diets for growing olive flounder Paralichthys olivaceus. The control diet was formulated to contain 65% sardine FM and four other replacement diets were formulated to replace FM with the plant proteins by 25, 30, 35 and 40% (designated FM25, FM30, FM35 and FM40, respectively). The replacement diets were added with three essential amino acids (lysine, methionine and threonine) to meet their requirements for the fish. Olive flounder (initial average weight, 96.8±0.2 g) were randomly distributed into 20 tanks (425 L each) at a density of 25 fish per tank. Four replicate groups of fish were fed one of the diets two times daily for 15 weeks. At the end of the feeding trial, no significant differences were found among all the fish groups in growth performance, feed utilization, nonspecific immune responses and hematological health parameters. Thus, this result indicates that the plant proteins with the three limiting amino acids could replace FM up to 40% in diets for growing olive flounder.