• The Korean Journal of Food And Nutrition
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• v.8 no.1
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• pp.37-42
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• 1995

The amino acid sequence of basic isozyme 55 of Horseradish Peroxidase (HRP E5) was determined by protein sequencing. HRP E5 consisted about 300 residues, and has a molecular weight of approximately 36,000 $\pm$ 500 dalton. The protein was rich In aspartic acid (14%), arginine(13%), and leucine(11%). The primary structure of HRP E5 was established by sequencing its tryptic (T1-T19) and lysylendopeptic (Al-A3) peptides. The sequence homology between HRP E5 and HRP C (neutral isozyme of horseradish peroxidase) is found to be more than 66%. The highest concentration of identical residues are found on residues 29~56, 90~123, and 155~173, but relatively low on 174~271.

• Korean Journal of Plant Taxonomy
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• v.52 no.4
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• pp.219-225
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• 2022

To elucidate the ancestry of the allopolyploids E. stevenii and E. boöphthona, I examined eleven isozyme loci and 24 morphological characters from 28 populations representing five related Euphorbia species from Australia. According to an analysis of genetic and morphological data, three diploid species differentiated recently, but two independent polyploid species are estimated to have differentiated a relatively long time ago. Fixed heterozygosity for most isozymes in E. stevenii and E. boöphthona strongly suggests that these two species are allopolyploids rather than autopolyploids. The isozyme profiles of E. stevenii indicate that it is an allopolyploid that evolved from interspecific hybridization between the diploid E. tannensis and unidentified or extinct tetraploid species. In addition, isozyme patterns strongly suggest that E. stevenii was one of the ancestors of E. boöphthona. However, E. boöphthona showed a large number of fixed alleles that were not detected in any other Australian Eremophyton species. The most likely hypothesis for the origin of E. boöphthona is that it was formed by hybridization and chromosomal doubling between an extinct diploid species and the hexaploid E. stevenii.

• Proceedings of the Korean Society of Crop Science Conference
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• 1991.05a
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• pp.24-25
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• 1991

• Proceedings of the Korean Society of Crop Science Conference
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• 1988.02a
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• pp.12-13
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• 1988

• Korean Journal of Soil Science and Fertilizer
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• v.7 no.4
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• pp.209-213
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• 1974

The isozymes of glutamic oxalacetic transaminase from young rice root were isolated by DEAE-cellulose column chromatography, and investigated some of their enzymic properties. Obtained results were summarized as follows: 1. 93 percent of GOT activity in rice root existed in supernatant fraction, and their specific activity exibited the same pattern. 2. The rice root contained two types of GOT isozyme; cationic and anionic GOT. It seemed that both of them were distributed in supernatant fraction. 3. GOT isozymes of rice root on the pH dependance showed their maximum activity at 7.4. 4. On the stability of GOT isozymes for temperature, anionic GOT was more unstable than cationic GOT. 5. Apparent Michaelis constant for L-aspartate of GOT isozymes from rice root showed 12-14mM in the cationic GOT and 16mM in the anionic GOT, respectively.

• Korean Journal of Food Science and Technology
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• v.19 no.5
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• pp.397-402
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• 1987

Two lipoxygenases (F-I and F-II) were purified from potato tubers by ammonium sulfate fractionation and ion-exchange column chromatographies. The purified isoenzymes were apparently homogeneous on polyacrylamide gel electrophoresis. Both enzymes showed a similar optimum pH of 5.5-6.0. From thermal inactivation experiments with the purified enzymes in the range of 50 to $65^{\circ}C$, D-values of 13.3 min and 4.3 min at $65^{\circ}C$, and z-values of $11.8^{\circ}C\;and\;10.3^{\circ}C$ were obtained respectively for F-I and F-II. By applying absolute reaction rate equation, thermodynamic parameters wire also determined for the activation part of the inactivation process.

• Journal of Life Science
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• v.20 no.3
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• pp.416-423
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• 2010

In this study, the properties and gene expression of the lactate dehydrogenase (EC 1.1.1.27, LDH) isozyme were studied in angelfish (Pterophyllum scalare) - known for their adaptation to the low oxygen environment of the tropics - which were acclimated to acute temperature change ($27{\pm}0.5{\rightarrow}18{\pm}0.5^{\circ}C$) and dissolved oxygen (DO) change ($6{\pm}1{\rightarrow}18\;ppm$) for 2 hours. The properties of the LDH isozymes were confirmed in the native-polyacrylamide gel electrophoresis, Western blot analysis and enzyme activity measurement. Liver- and eye-specific Ldh-C gene were expressed in liver, eye and brain tissues. Through Western blot analysis, the LDH $A_4$ isozyme was shown to have a more cathodal mobility relative to the $B_4$ isozyme. In the liver tissue, the LDH $A_4$ isozyme increased with temperature drop while the $B_4$ isozyme decreased. The LDH $A_4$ and $C_4$ isozymes increased with DO increment, while the $B_4$ isozyme decreased. In the eye tissue, the LDH $A_4$ and B4 isozymse increased with temperature drop while the $B_4$ isozyme decreased. The LDH $A_4$ and $B_4$ isozymes increased with DO increment, but the $C_4$ isozyme and isozymes including the subunit C decreased. In the heart tissue, LDH activity increased with DO increment, as well as the LDH $B_4$ isozyme. In the brain tissue, the LDH $A_4$ and $B_4$ isozymes increased with temperature drop. The LDH $B_4$ isozyme increased with DO increment. Accordingly, since the liver- and eye-specific Ldh-C are influenced by changes in DO and the LDH $B_4$ and $C_4$ isozymes are relatively controlled in the liver and eye tissues, the $C_4$ isozyme can be considered to have a lactate oxidase function.

• Journal of Korean Society of Forest Science
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• v.68 no.1
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• pp.32-36
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• 1985

Megagametophyte tissues of Pinus densiflora were subjected to study the inheritance of acid phosphatase (ACP), alcohol dehydrogenase (ADH) and catalase (CAT) isozymes by starch gel zone-electrophoresis. At least three or four zones were segregated for ACP isozyme. However, as one isozyme of ACP-A zone was separated clearly, only that isozyme was analysed. Five isozyme phenotypes (A1-A5), observed in ACP-A zone, were segregated to a simple Mendelian ratio, suggesting that these are controlled by five codominant alleles existed at ACP-A locus. Two zones of activity were segregated in the gels after staining for ADH, the more anodal zone (ADH-A) of the two was invariant in our materials. Three isozyme phenotypes (B1-B3) were observed in ADH-B zone and these variants showed a 1:1 segregation pattern, suggesting that each variant is controlled by three codominant alleles at ADH-B locus. A total of five isozyme phenotypes, composed of multiple bands, were observed in CAT isozyme. The segregation of these phenotypes in heterozygous trees did not show any significant deviation from a 1:1 segregation. Therefore, the genetic control of CAT isozyme in Pinus densiflora seeds seems to be based on a single locus (CAT-A) with Five codominant alleles ($A_1-A_5$).

• Journal of Life Science
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• v.24 no.2
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• pp.118-127
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• 2014

The kinetic properties and isozyme expression of lactate dehydrogenase (EC 1.1.1.27; LDH) in tissues from Rana catesbeiana I and II collected from February (I) and August (II) were studied. LDH activities, A4 isozyme, and LDH/citrate synthase (EC 4.1.3.7; CS) were high in skeletal muscle from R. catesbeiana I, and LDH $B_4$ isozyme increased in several tissues of R. catesbeiana II. In particular, LDH activities were high in heart and brain tissues from R. catesbeiana II. LDH eye-specific C isozyme, detected by native polyacrylamide gel electrophoresis after immunoprecipitation, was expressed in eye tissue and was more similar to the $B_4$ than $A_4$ isozyme. LDH $A_4$ isozyme was purified by oxamate-linked affinity chromatography, and the molecular weight of subunit A was 32.0 kDa. In R. catesbeiana II, levels of $Km^{PYU}$, $Vmax^{LAC}$, and tolerance to lactate of LDH were high in all tissues, and $Vmax^{PYU}$ of LDH in heart and brain tissue was highly detected. Purified $A_4$ isozyme and LDH in eye tissue were highly tolerate compared to others. The $Km^{LAC}$ value was highly measured compared to $Km^{PYU}$. The degree of inhibition by 10 mM of pyruvate on LDH activities in tissues from R. catesbeiana I and II was more pronounced as the ratio of subunit B increased. As a result, characteristic expression of LDH eye-specific C was found in R. catesbeiana. Anaerobic metabolism seemed to predominate as the LDH of skeletal muscle from I showed higher activity. It also appeared that R. catesbeiana II adapted well to incremental increases in LDH B, becoming tolerant to the lactate of LDH in tissues.

• International Journal of Industrial Entomology and Biomaterials
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• v.8 no.2
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• pp.189-194
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• 2004

Amylase isozyme based three multivoltine viz., N+p, Np, N+ $p^{cho}$ and two bivoltine-D6+p, D6p syngenic lines (Syn. L) were developed from germplasm (GP) stocks Nistari (N) and D6 respectively. haemolymph isozyme pattern at pH 7.0 and 8.5 depicted a total 11 number (Am $y_{1 to 6}$ at pH 7.0 and Am $y^{l to 5}$ at pH 8.5) of native proteins (NP) of various sizes are amylase isozyme expressers. Among eleven NPs, two NPs of 770 kDa (Am $y^{6}$ at pH 7.0) and 376 kDa (Am $y^3$ at pH 8.5) are $\alpha$-amylase expressers and remaining NPs of 370, 364, 350, 329 and 274 kDa at pH 7.0 and 206, 292, 416, 725 kDa at pH 8.5 are $\beta$-amylase expressers. Accordingly, digestive juice amylase isozyme pattern at aforesaid pH also depicted a total number of 10 NPs (Am $y^{1 to 5}$) at each pH 7.0 and 8.5 are amylase expressers of which NP of 387 kDa (Am $y^4$ at pH 7.0) and 780 kDa (Am $y^{5}$ at pH 8.5) are a-amylase expresser. Remaining NPs of 338,297 ＆ 216 kDa at pH 7.0 and 370, 341, 329 ＆302 kDa at pH 8.5 are $\beta$-amylase expresser. Recurrent backcross lines (RBL) viz., N+pRBL and NpRBL were developed through introgression of high shell weight character (a multigenic trait) to be used further for congenic line (Con. L) development and to understand any association with introgressed character. Isozyme pattern in haemolymph of RBLs depicted only one $\alpha$-amylase of 770 kDa at pH 7.0 and 376 kDa at pH 8.0 with three and four respective $\beta$-amylase bands but in bivoltine lines numbers of $\beta$-amylase bands vary between 1 to 2 at aforesaid pH. Variability was also observed in digestive juice of multivolitine and its RBLs but bivoltine lines express null activity at both pH except appearance of one very week $\alpha$-amylase band D6+p at pH 8.5. Overall study suggests that not a single NP at both pH is common for expression of any band of amylase isozyme i.e., a totally different set of proteins are the amylase isozyme expresser at specific pH and no molecular factor of amylase is associated in developed RBLs which showed improvement on survival, single cocoon shell weight (SCSW) and single filament length over receptor parents.s.s.s.