• 대한생식의학회:학술대회논문집
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• 2004.11a
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• pp.44-45
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• 2004

• Proceedings of the Zoological Society Korea Conference
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• 2001.04a
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• pp.64.2-64
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• 2001

No Abstract, See Full Text

• Proceedings of the Zoological Society Korea Conference
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• 2001.04a
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• pp.65.2-65
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• 2001

No Abstract, See Full Text

• Fisheries and Aquatic Sciences
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• v.13 no.2
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• pp.102-111
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• 2010

This study was conducted to investigate the optimal conditions of collagen extraction from scales of yellowfin tuna (Thunnus albacares) using surface response methodology. Four independent variables of NaOH concentration and pretreatment fime in alkali pretreatment and enzyme concentration and treatment time in enzyme hydrolysis were used to predict a model equation for the collagen yield. The determinant coefficient ($R^2$) for the equation was 0.906. The values of the independent variables for the maximum yield were 0.32 N NaOH, 16.38 h alkali pretreatment time, 0.18% enzyme concentration, and 31.02 h enzyme treatment time. In the physicochemical properties of tuna scale collagen, sodium dodecyl sulfate-polyacrylamide gel electrophoresis of tuna scale collagen showed the same migration distances as that of calf skin collagen. The amide A, I, II, and III regions of tuna scale collagen in Fourier transform infrared measurements were shown in the peaks of 3,414 $cm^{-1}$, 1,645 $cm^{-1}$, 1,553 $cm^{-1}$, and 1,247 $cm^{-1}$, respectively. The amount of imino acids in tuna scale collagen was 18.97% and the collagen denaturation temperature was $33^{\circ}C$. The collagen solubility as a function of NaCl concentration decreased to 4% NaCl (w/v) and the collagen solubility as a function of pH was high at pH 2-4 and sharply decreased from pH 4 to pH 7. Viscosity of the collagen solution decreased continuously until $30^{\circ}C$ and this decreasing rate slowed in the temperature range of $35-50^{\circ}C$.

• Journal of the Korean Society of Laryngology, Phoniatrics and Logopedics
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• v.21 no.1
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• pp.32-36
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• 2010

Background : Vocal fold injection using autologous material (fat or collagen) is very useful. However, Autologous material have variable resorption times and results, Plasma gel is a new injection material. The purpose of this study is to introduce a new injection material and discuss the effectiveness and complications. Subjects and Method: Eleven cases with vocal cord paralysis were analyzed after plasma gel injection, The plasma gel was acquired from patient's own blood. The preoperative and postoperative parameters including maximum phonation time (MPT) and subject aspiration score were analyzed. Results: There was a significant improvement in MPT and aspiration score in the case of vocal cord palsy. There was only one laryngeal complication. Conclusion : According to these preliminary results, the injection laryngoplasty with Plasma gel is a simple, safe, cheap procedure for temporally vocal fold palsy.

• Korean Journal of Acupuncture
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• v.37 no.2
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• pp.88-96
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• 2020

Objectives : The purpose of this study was to investigate the anti-oxidant and anti-aging effect of the seed of Euphorbia lathyris L. extracted by supercritical CO₂. Methods : Human dermal fibroblast cells dosed with the extract from Euphorbia lathyris L. were harvested and the intracellular proteome was analyzed to examine the expression of proteins related collagen synthesis pathway, metalloproteinases (MMPs), extracellular matrix (ECM)-cell interaction, cytokines, and antioxidant enzymes by 2-dimensional gel electrophoresis. Results : Fatty acid analysis of the extract from Euphorbia lathyris L. showed oleic acid was 84% and linoleic acid was 4.1%. Antioxidative effect was about 53% by beta carotene bleaching assay. In 2-dimensional polyacrylamide gel electrophoresis (2-D PAGE) analysis, fifteen protein changes in five mechanisms which were collagen synthesis pathway, MMPs, ECM-cell interaction, cytokines, and antioxidant enzymes were analyzed. Conclusions : This study suggests the supercritical extraction from the seed of Euphorbia lathyris L. could be used as anti-oxidant substances for pharmacopuncture.

• Food Science of Animal Resources
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• v.34 no.2
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• pp.151-157
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• 2014

This study investigated the effects of three proteases (trypsin, pepsin and chymotrypsin) on the hydrolysis efficiency of porcine placenta and the molecular weight (Mw) distributions of the placental hydrolysates. Because placenta was made up of insoluble collagen, the placenta was gelatinized by applying thermal treatment at $90^{\circ}C$ for 1 h and used as the sample. The placental hydrolyzing activities of the enzymes at varying concentrations and incubation times were determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and gel permeation chromatography (GPC). Based on the SDS-PAGE, the best placental hydrolysis efficiency was observed in trypsin treatments where all peptide bands disappeared after 1 h of incubation as compared to 6 h of chymotrypsin. Pepsin hardly hydrolyzed the placenta as compared to the other two enzymes. The Mw distribution revealed that the trypsin produced placental peptides with Mw of 106 and 500 Da. Peptides produced by chymotrypsin exhibited broad ranges of Mw distribution (1-20 kDa), while the pepsin treatment showed Mw greater than 7 kDa. For comparisons of pre-treatments, the subcritical water processing (37.5 MPa and $200^{\circ}C$) of raw placenta improved the efficiency of tryptic digestions to a greater level than that of a preheating treatment ($90^{\circ}C$ for 1 h). Consequently, subcritical water processing followed by enzymatic digestions has the potential of an advanced collagen hydrolysis technique.

• The korean journal of orthodontics
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• v.9 no.1
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• pp.9-14
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• 1979

The purpose of this study was to pursue the biosynthesis of proteins of human and bovine periodontal ligaments in vitro system. The excised periodontal ligaments from human and bovine were incubated in Krebs-glucose medium containing $^3H$-proline. After incubation the incubated periodontal ligaments were homogenized and the proteins were treated with 0.1%sodium dodecyl sulfate and $\beta$-mercaptoethanol. Separation of the protein fractions was performed with agarose gel column chromatography and SDS acrylamide gel electrophoresis. The results indicated as follow: 1. Only a small percentage of $^3H$-proline incorporated into proteins was hydroxylated to $^3H$-hydroxyproline. 2. The labeled proteins in periodontal ligaments showed a wide distribution of molecular weight. But only small amounts of labeled protein were found that were characteristics of the molecular weight of collagen. 3. In all of the combined fractions of gel filtration, the degree of hydroxylation was small.

• Journal of Periodontal and Implant Science
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• v.23 no.2
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• pp.219-227
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• 1993

The purpose of the present study was to evaluate the effects of 5% tetracycline(Tc) with or without citric acid on periodontally diseased root surfaces. Six single-rooted teeth extracted from one patient was selected and received thorough scaling and root planning, followed by saline irrigation. Each one tooth was divided into eight fragments with a thin separating disc. Total 48 fragments were prepared and setted into 4 groups for this study. Group I (control group)were treated with saline. Group II were treated with 5% Tc gel. Group III were treated with 33% citric acid-5% Tc gel. Group IV were treated with Tc solution. All the specimens are evaluated under Scanning Electron Microscope(SEM). Group I showed large amount of debris in spite of thorough scaling and root planing, but Group II, III & IV showed clean and soft root surface texture. In higher magnification(x3, 000), Group II, III & IV showed nunmerous dentinal tubules, especially Group IV showed collagen fibrils. In the present study, Tc gel and Tc gel with citric showed clinically successful result when treated on periodontally diseased root surface, in vitro.

• Food Science of Animal Resources
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• v.32 no.3
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• pp.316-322
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• 2012

This study was conducted to evaluate the effects of soaking pH and extraction temperature on the physicochemical properties of chicken skin gelatin. In order to extract gelatin from chicken skin, the chicken skin was soaked at various pH ranges (1-13) and was extracted at 75 and $100^{\circ}C$. For the rate of weight increase, the highest value was obtained from two pH ranges (1-2 and 12-13). In addition, the rate of weight increase was affected by soaking time. The alkali treatments had greater crude protein content as well as total extraction yield compared to the acid process (p<0.05), and the increased extraction temperature resulted in a significant (p<0.05) increase of crude protein content and total extraction yield. All treatments showed ${\alpha}1$ and ${\alpha}2$ chains derived from type I collagen on SDS-PAGE. The pH value and color of gelatin gel (6.67%) were affected by soaking pH and extraction temperature. Chicken skin gelatin gel extracted at $75^{\circ}C$ after soaking at a pH of 2 had the highest melting point (p<0.05) and gel strength among all treatments. Although the chicken skin treated with the alkali process had a higher yield, a lower extraction temperature following the acid process would be better for obtaining superior gelatin from chicken skin.