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일 최저기온 공간내삽을 위한 지형기후학적 최적 공간규모
정유란,서희철,윤진일,이광회 한국농림기상학회 2003 한국농림기상학회지 Vol.5 No.4
Cold air accumulation plays a critical role in formulating daily minimum temperature in complex terrain on radiative cooling nights, and spatial interpolation can be improved by accommodating this important topoclimatic variable. Little is known about the spatial scale for computing cold air accumulation which influences daily minimum temperature. Air temperature was measured at 10-minute intervals during September 2002 - February 2003 at eight locations within a 1 by 1 km hilly orchard area. Minimum temperature data for suspected radiative cooling nights were collected, and the deviations from reference observations at a near-by KMA automated weather station were calculated. A digital elevation model with a 10m cell size was used to calculate the cold air accumulation at 8 locations. Zonal averages of the cold air accumulation were computed for each location by increasing the cell radius from 1 to 10. Temperature deviations were regressed to a common logarithm of the smoothed averages of cold air accumulation to derive a linear relationship between the local temperature deviation and the site topography. The highest coefficient of determination (r² = 0.78) was found at a cell radius of 5, which corresponds to an approximately 1 ha boundary surrounding the point of interest.
Chung, Kwang-Hoe,Kim, Doo-Sik 생화학분자생물학회 1993 한국생화학회지 Vol.26 No.4
A fibrinolytic enzyme was purified to homogeneity from the venom of Korean Salmosa snake Agkistrodon halys by a combination of benzamidine-Sepharose affinity chromatography and FPLC Mono Q ion exchange fractionation. The purified enzyme is a glycoprotein and migrates as a single band with molecular mass of 51,000 Da on SDS-polyacrylamide gel electrophoresis. The native molecular weight was determined to be 52,000 Da by FPLC gel filtration. The fibrinolytic enzyme is characterized by its isoelectric point of 3.52. Amino terminal sequence of the enzyme was identified to be Val-Ile-Gly-Gly-Asp-Glu-Asn-Ile-Asn-Glu-His-Arg-Phe-Leu-Val-Ala-Met, which is homologous to that of protein C activator from Agkistrodon contortrix.
Chung, Kwang-Hoe,Kim, Doo-Sik 생화학분자생물학회 1993 한국생화학회지 Vol.26 No.4
The fibrinolytic enzyme of 51,000 Da isolated from the venom of Agkistrodon halys lyses fibrinogen and fibrin polymer in the absence of plasminogen without having thrombinlike activity. Treatment of the enzyme with diisopropyl fluorophosphate or phenylmethylsulfonyl fluoride resulted in complete loss of the fibrinolytic activity, suggesting that the enzyme is a member of serine protease family. Proteolytic activity of the enzyme is also inhibited by incubation with metal ions such as $Zn^{2+}$, $Cu^{2+}$, $Cd^{2+}$, $Li^{2+}$, and $Co^{2+}$. The enzyme is relatively stable at room temperature and its maximal catalytic activity is attained at pH 8.0, $37^{\circ}C$. The ${\alpha}$ chain of fibrinogen or fibrin polymer is more sensitive to the proteolytic degradation by the enzyme than the ${\beta}$ chain, while the ${\gamma}$ chain is not affected at all. Hydrolysis of the synthetic peptide substrates including N-benzoyl-Phe-Val-Arg-p-nitroanilide, which is a specific substrate for angiotensin I-converting enzyme, suggests the venom fibrinolytic enzyme cleaves after arginine residue. The enzyme was not able to hydrolyze human serum albumin, plasminogen, thrombin, immunoglobulin, and tissue-type plasminogen activator. Since the enzyme is active in human plasma and the degree of fibrinolysis was proportional to the amount of enzyme added, it is postulated that the enzyme can mediate fibrinolytic function in vivo.
Kwang Hoe Chung,Doo Sik Kim 생화학분자생물학회 1993 BMB Reports Vol.26 No.4
The fibrinolytic enzyme of 51,000 Da isolated from the venom of Agkistrodon halys lyses fibrinogen and fibrin polymer in the absence of plasminogen without having thrombinlike activity. Treatment of the enzyme with diisopropyl fluorophosphate or phenylmethylsulfo-nyl fluoride resulted in complete loss of the fibrinolytic activity, suggesting that the enzyme is a member of serine protease family. Proteolytic activity of the enzyme is also inhibited by incubation with metal ions such as Zn^(2+), Cu^(2+), Cd^(2+), Li^(2+) +, and Co^(2+). The enzyme is relatively stable at room temperature and its maximal catalytic activity is attained at pH 8.0, 37℃. The α chain of fibrinogen or fibrin polymer is more sensitive to the proteolytic degradation by the enzyme than the β chain, while the γ chain is not affected at all. Hydrolysis of the synthetic peptide substrates including N-benzoyl-Phe-Val-Arg-p-nitroanilide, which is a specific substrate for angiotensin I-converting enzyme, suggests the venom fibrinolytic enzyme cleaves after arginine residue. The enzyme was not able to hydrolyze human serum albumin, plasminogen, thrombin, immunoglobulin, and tissue-type plasminogen activator. Since the enzyme is active in human plasma and the degree of fibrinolysis was proportional to the amount of enzyme added, it is postulated that the enzyme can mediate fibrinolytic function in vivo.
Fibrinolytic and Cogulation Activities of Korean Snake Venoms
Chung, Kwang-Hoe,Kim, Doo-Sik 생화학분자생물학회 1992 한국생화학회지 Vol.25 No.8
The action of snake venoms from 3 different kinds of Korean venomous species (Agkistrodon halys brevicaudus, Agkistrodon saxatilis, Agkistrodon ussuriensis) on the haemostasis and fibrinolytic system was studied and compared with other two venoms of Agkistrodon rhodostoma, Malayan Pit Viper and Agkistrodon halys blomhoffi, Japanese Mamushi. The coagulation activity, fibrinolytic, fibrinogenolytic, and amidolytic activity were determined. Fibrinogen clotting activity in the venoms of Agkistrodon saxatilis and Agkistrodon ussuriensis were 1.0 and 3.5 NIH U/mg. However, it was not able to detect the fibrinogen clotting activity from. the venom of Agkistrodon halys (Korean Salmosa) during prolonged incubation. Polyacrylamide gel electrophoretic patterns of these venoms were quite different from each other. After removal of SDS from the gel with Triton X-100, the fibrinolytic activities in the gel could be directly detected by the fibrin-agar zymographic assay method. The venom of Agkistrodon halys has shown at least two distinct fibrinolytic enzymes (51 Kd and 33 Kd, Agkistrodon saxatilis has three (47 Kd, 33 Kd, and 28 Kd), and Agkistrodon caliginosus has two (38 Kd and 33 Kd). No plasminogen activation activity was observed in any of the venoms of Korean poisonous snakes.
Fibrinolytic and Cogulation Activities of Korean Snake Venoms
Kwang Hoe Chung,Doo Sik Kim 생화학분자생물학회 1992 BMB Reports Vol.25 No.8
The action of snake venoms from 3 different kinds of Korean venomous species (Agkistrodon halys brevicaudus, Agkistrodon saxatilis, Agkistrodon ussuriensis) on the haemostasis and fibrinolytic system was studied and compared with other two venoms of Agkistrodon rhodostoma, Malayan Pit Viper and Agkistrodon halys blomhoffi, Japanese Mamushi. The coagulation activity, fibrinolytic, fibrinogenolytic, and amidolytic activity were determined. Fibrinogen clotting activity in the venoms of Agkistrodon saxatilis and Agkistrodon ussuriensis were 1.0 and 3.5 NIH U/㎎. However, it was not able to detect the fibrinogen clotting activity from. the venom of Agkistrodon halys (Korean Salmosa) during prolonged incubation. Polyacrylamide gel electrophoretic patterns of these venoms were quite different from each other. After removal of SDS from the gel with Triton X-100, the fibrinolytic activities in the gel could be directly detected by the fibrin-agar zymographic assay method. The venom of Agkistrodon halys has shown at least two distinct fibrinolytic enzymes (51 Kd and 33 Kd, Agkistrodon saxatilis has three (47 Kd, 33 Kd, and 28 Kd), and Agkistrodon caliginosus has two (38 Kd and 33 Kd). No plasminogen activation activity was observed in any of the venoms of Korean poisonous snakes.