• Proceedings of the Korean Society for Agricultural Machinery Conference
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• 1993.10a
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• pp.1243-1253
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• 1993

Visual features of a mushroom(Lentinus Edodes L) are critical in sorting and grading as most agricultural products are. Because of its complex and various visual features, grading and sorting of mushrooms have been done manually by the human expert. Though actions involved in human grading looks simple, a decision making undereath the simple action comes form the results of the complex neural processing of the visual image. And processing details involved in the visual recognition of the human brain has not been fully investigated yet. Recently, however, an artificial neural network has drawn a great attention because of its functional capability as a partial substitute of the human brain. Since most agricultural products are not uniquely defined in its physical properties and do not have a well defined job structure, a research of the neuro-net based human like information processing toward the agricultural product and processing are widely open and promising. In this pape , neuro-net based grading and sorting system was developed for a mushroom . A computer vision system was utilized for extracting and quantifying the qualitative visual features of sampled mushrooms. The extracted visual features and their corresponding grades were used as input/output pairs for training the neural network and the trained results of the network were presented . The computer vision system used is composed of the IBM PC compatible 386DX, ITEX PFG frame grabber, B/W CCD camera , VGA color graphic monitor , and image output RGB monitor.

• Journal of Microbiology and Biotechnology
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• v.16 no.6
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• pp.988-992
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• 2006

The ptsHI operon from Leuconostoc mesenteroides ssp. mesenteroides SY1 (L. mesenteroides SY1), a strain isolated from kimchi, was cloned and characterized. The ptsH open reading frame (ORF) was 273 bp in size, which can encode a protein of 90 amino acid residues with a molecular weight of 9,212 Da. The pfsI ORF was 1,719 bp in size, which was capable of encoding a protein of 572 amino acids with a molecular mass of 62,549 Da. ptsH and pfsI genes were transcribed as a single transcript of 2.0 kb in size regardless of carbon sources, supporting the operon structure. Although the deduced amino acid sequences of the HPr and EI were highly homologous with those of other Gram-positive bacteria, an additional amino acid (glutamine at the $3^{rd}$ amino acid) was present in HPr from L. mesenteroides SY1. Phosphorylation sites of HPr included the histidine residue ($16^{th}$) and serine residue ($47^{th}$). Mutant HPrs, in which each phosphorylation site was mutated into alanine, were obtained, and phosphorylation with HPr and mutated HPrs showed that HPr was phosphorylated at the serine residue ($47^{th}$) by HPr kinaseiphosphorylase (HPr K/P).

• The Journal of Korean Society of Virology
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• v.28 no.1
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• pp.53-62
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• 1998

Human papillomavirus (HPV) 16, E7 proteins derived from the prototype (Bac73) and natural variant (Bac101) E7 open reading frame were produced in Sf9 insect cells. The variant E7 gene occurred naturally by substitution mutation at the position of 88 nucleotide, resulting serine instead of asparagine. Using E7 specific monoclonal antibody (VD6), both E7 proteins were identified in recombinant baculovirus infected SF9 cells. Radiolabelling and immunoprecipitation analysis revealed that both E7 proteins were phosphoproteins. Immunostaining result showed that E7 proteins were mainly localized in the cytoplasm. Nuclear form of E7 proteins was also detected after a sequential fractionation procedure for removing chromatin structure. Considering that the VD6 recognition site in E7 protein is located within 10 amino acid at the N-terminus, this region appears to be blocked by the nuclear component. Western blot analysis revealed that nuclear form was more abundant than cytoplasmic E7 proteins. Time course immunostaining showed that the primary location of E7 protein was the nucleus and exported to the cytoplasm as proteins were accumulated. These events occurred similarly in both Bac73 and Bac101 infected Sf9 cells, suggesting that these two proteins may have similar biological functions.

• Asian-Australasian Journal of Animal Sciences
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• v.18 no.5
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• pp.723-727
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• 2005

Ghrelin is a novel growth-hormone-releasing acylated peptide, which has been purified and identified in rat stomach. In the present study, the full-length sequence of bovine ghrelin cDNA was cloned by RT-PCR. The bovine ghrelin cDNA sequence derived in the present study included a 348 bp open reading frame and a 137 bp 3'UTR. The putative amino acid sequence of bovine prepro-ghrelin consisted of 116 amino acids, which contained the 27-amino acid ghrelin. The sequence analysis of the bovine ghrelin gene revealed that an intron existed between Gln$^{13}$ and Arg$^{14}$ of ghrelin. This exon-intron boundary matched the GT-AG rule of the splicing mechanism. Compared with rats, which have two tandem CAG sequences in the 3'end of intron, bovine ghrelin genome has only one CAG sequence. Therefore, although rats can produce 28 amino acid-ghrelin and 27 amino acid-des-Gln$^{14}$-ghrelin by alternative splicing, ruminant species, including bovines, might be able to produce only one type of ghrelin peptide, des-Gln$^{14}$-ghrelin. The influence of aging on plasma ghrelin concentration was also examined. Plasma ghrelin concentration increased after birth to approximately 600 days of age, and then remained constant.

• Asian-Australasian Journal of Animal Sciences
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• v.21 no.11
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• pp.1673-1679
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• 2008

In order to study the biological function of gapdh gene in yak, and prove whether the gapdh gene was a useful intra-reference gene that can be given an important role in molecular biology research of yak, the cDNA sequence encoding glyceraldehyde-3-phosphate dehydrogenase from yak was cloned by the RT-PCR method using gene specific PCR primers. The sequence results indicated that the cloned cDNA fragment (1,008 bp) contained a 1,002 bp open reading frame, encoding 333 amino acids (AAs) with a molecular mass of 35.753 kDa. The deduced amino acids sequence showed a high level of sequence identity to Bos Taurus (99.70%), Xenopus laevis (94.29%), Homo sapiens (97.01%), Mus musculus (97.90%) and Sus scrofa (98.20%). The expression of yak's gapdh gene in heart, spleen, kidney and brain tissues was also detected; the results showed that the gapdh gene was expressed in all these tissues. Further analysis of yak GAPDH amino acid sequence implied that it contained a complete glyceraldehyde-3-phosphate dehydrogenase active site (ASCTTNCL) which ranged from 148 to 155 amino acid residues. It also contained two conserved domains, a NAD binding domain in its N-terminal and a complete catalytic domain of sugar transport in its C-terminal. The phylogenetic analysis showed that yak and Bos taurus were the closest species. The prediction of secondary structures indicated that GAPDH of yak had a similar secondary structure to other isolated GAPDH. The results of this study suggested that the gapdh gene of yak was similar to other species and could be used as the intra-reference to analyze the expression of other genes in yak.

• Korean Journal of Microbiology
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• v.38 no.4
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• pp.230-230
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• 2002

Class Ⅲ chitin synthases in filamentous fungi are important for hyphal growth and differentiation of several filamentous fungi. A genomic clone containing the full gene encoding Chs4, a class Ⅲ chitin synthase in Penicillium chrysogenum, was cloned by PCR screening and colony hybridization from the genomic library. Nucleotide sequence analysis and transcript mapping of chs4 revealed an open reading frame (ORF) that consisted of 5 exons and 4 introns and encoded a putative protein of 915 amino acids. Nucleotide sequence analysis of the 5′flanking region of the ORF revealed a potential TATA box and several binding sites for transcription activators. The putative transcription initiation site at -716 position was identified by primer extension and the expression of the chs4 during the vegetative growth was confirmed by Northern blot analysis. Amino acid sequence analysis of the Chs4 revealed at least 5 transmembrane helices and several sites for past-transnational modifications. Comparison of the amino acid sequence of Chs4 with those of other fungi showed a close relationship between P chrysogenum and genus Aspergillus.

• Journal of the Korean Society of Clothing and Textiles
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• v.16 no.4 s.44
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• pp.357-369
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• 1992

The purpose of this study was to clarify the relationship between the Ideal Beauty of Body and the Form of Dress, and to analyze its historical perspectives. First of all, the concept of the Ideal Beauty of Body, the definition of Dress Form, and the method and system to clarify Dress Form were depicted. Based on this frame work, the Form of Dress related to the Ideal Beauty of Body was described historically. For this purpose, documentary research were conducted and representative photography and paintings were used. The analysis was limited to the female one-Piece dress from Ancient Egypt, Greece, Rome, Byzantine, Gothic, Renaissance, Baroque, Rococo, Naoclassicism, and to Romanticism. The results were as follows: 1. The Ideal Beauty of Body was found to be different throughout history and to be intimate- ly linked with fashionable dress. 2. The Form of Dress consisted of four basic components: The form of body itself, the form of clothing itself, the method of wearing, and the relationship between body and clothing. 3. The standards for classification of body form were body structure, body type, body proportion, posture, and movement. Clothing form was generally classified into flat type (unstructured type) and three dementional type (structured type); flat type was subclassified into draped type and tunic type. The method of wearing was classified into attached type, tying-up type, wrap·around type, pull-over type, open type and plastistic type. The relationship between body and clothing after wearing was generally classified into body priority type and clothing priority type. The clothing priority type was further divided into body exaggeration type and body concealment type; Body exaggeration type was further divided into upward type, downward type, forward type, backward type, right type and constriction type. 4. The pursuit of venus coelestis, metaphysical body part, ectomorphic body type, flat type clothing, body priority type; the pursuit of Venus Naturalis, physical body part, endomorphic body type, three dementional type clothing, clothing priority type proved to be closely related respectively by the historical study on the Ideal Beauty of Body and the Form of Dress.

• Proceedings of the Korean Institute of Electrical and Electronic Material Engineers Conference
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• 2002.11a
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• pp.596-602
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• 2002

An easy elevator for learning originated is opened to compare the existed learning equipment, and it had a high studying efficient that the sequence control circuit can opens and closes with the wire. The structure of equipment to be controlled from the first floor to the fifth floors is demonstrated a constructive apparatus by a lamp atc to express the function of the open-close of the door according to the cage moving with a mechanical actuation of the forward-reverse breaker and the motor of load and a mechanical actuation of hand-operation control components of push-button S/W and L/S and relay etc. These components let connects each other in order to control of the elevator function with the auto program and the designed sequence control circuit. Consequent1y the process of these functions of 1~5steps could operates the cage with an auto program of the elevator and the sequence control circuit. The sequence control circuit is controlled by the step of forward and reverse to follow as that the sensor function of the L/S1~L/S5 let posit with the control switchs of S/W1~S/W5 of PLC testing panel and switchs of S/W1~S/W5 installed on the transparent acryl plate of the frame. In here, improved apparatus is a hand-auto operation combined learning equipment to study the principle and a technique of the originated sequence control circuit and the auto program of PLC.

• Molecules and Cells
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• v.19 no.3
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• pp.328-333
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• 2005

Small heat shock proteins (sHSPs) are widely distributed, and their function and diversity of structure have been much studied in the field of molecular chaperones. In plants, which frequently have to cope with hostile environments, sHSPs are much more abundant and diverse than in other forms of life. In response to high temperature stress, sHSPs of more than twenty kinds can make up more than 1% of soluble plant proteins. We isolated a genomic clone, NtHSP18.3, from Nicotiana tabacum that encodes the complete open reading frame of a cytosolic class I small heat shock protein. To investigate the function of NtHSP18.3 in vitro, it was overproduced in Escherichia coli and purified. The purified NtHSP18.3 had typical molecular chaperone activity as it protected citrate synthase and luciferase from high temperature-induced aggregation. When E. coli celluar proteins were incubated with NtHSP18.3, a large proportion of the proteins remained soluble at temperatures as high as $70^{\circ}C$. Native gel analysis suggested that NtHSP18.3 is a dodecameric oligomer as the form present and showing molecular chaperone activity at the condition tested. Binding of bis-ANS to the oligomers of NtHSP18.3 indicated that exposure of their hydrophobic surfaces increased as the temperature was raised. Taken together, our data suggested that NtHSP18.3 is a molecular chaperone that functions as a dodecameric complex and possibly in a temperature-induced manner.

• BMB Reports
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• v.33 no.6
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• pp.483-492
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• 2000

The Herpes simplex virus type 1 (HSV-1) strain F glycoprotein H (gH) gene in the pHLB-4 plasmid was recombinated into a baculovirus expression vector (lacZ-HcNPV) to construct a recombinant virus GH-HcNPV expressing gH. The sequences of gH and its expression were analyzed. The gH gene was located in the 6.41 kb BglII fragment. The open reading frame (ORF) of the gH gene was 2,517 bp and codes 838 amino acid residues. Insect cells infected with this recombinant virus synthesized a high level of the matured and gX-gH fusion protein with approximately 112 kDa. The fusion gH protein was localized on the membrane of the insect cells as seen by using immunofluorescence assay and accumulated in the cultured media by the SDS-PAGE and immunoprecipitation assays. The amino acid sequence presents additional characteristics compatible with the structure of a viral glycoprotein: signal peptide, putative glycosylation sites and a long C-terminal transmembrane sequence. Antibodies raised in mice to this recombinant protein recognized viral gH and neutralized the infectivity of HSV-1 in vitro. These results demonstrate that it is possible to produce a mature protein by gene transfer in eukaryotic cells, and indicate the utility of the HcNPV-insect cell system for producing and characterizing eukaryotic proteins. Furthermore, the neutralizing antibodies would appear to protect mice against HSV; accordingly, this particular recombinant protein may be useful in the development of a subunit vaccine.