온도, pH및 염도 stress가 굴(Crassostrea gigas)의 malate dehydrogenase isozyme에 미치는 영향을 전기영동법으로 분석하였다. 대조군의 MDH isozyme은 2개의 band가 양극 쪽으로 이동되어 분리되었다. 각 실험 온도와 pH를 12시간 노출시킨 실험군에서는 1개의 band만 양극 쪽에서 분리되었고, 24시간과 48시간 노출한 실험군에서는 2개의 band가 모두 양극 쪽에서 분리되었다. 염분 농도가 5ppt

파밤나방(Spodoptera exigua(H bner))의 유전지표를 결정하기 위해 17종 동위효소의 좌위수, 대립유전자빈도 및 각 효소의 4차구조가 분석되었다. 총 분석된 좌우수는 30개였으며, 이중 70.0%가 다형유전좌위를 보였다. 좌위당 유효대립유전자수는 1.72개였고 평균이형접합율()은 32.8%로 추정되었다. 조사된 집단의 동계교배효과는 (F)는 21.0%이었다.

This study was planned to identify the effect of low-temperature stress on Alcohol dehydrogenase(ADH) isozyme in sixteen varieties of Italian ryegrass using starch gel electrophoresis. The specific electrophoretic zymograms of each variety were observed b

The amino acid sequence of basic isozyme E5 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±500 dalton. The protein was rich in aspartic acid (14%), arginine (13%), and leucine(ll%). The primary structure of HRP E5 was established by sequencing its tryptic(T_1-T_19) and lysylendopeptic(A_1-A_3) 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.

이탈리안 라이그라스 37개 품종을 대상으로 ADH와 Esterase 의 Isozyme을 Starch gel 전기영동법을 이용하여 분리한 후 염색하여 품종간 band 의 차이점을 비교하였다. 1. ADH isozyme은 Rf 0.60과 0.63 두 개의 band zone으로 나타났으며 Rf0.60이 main band이었다. 2. ADH isozyme의 banding pattern은 5개의 type으로 구별이 되었는데 type I은 7개품종, type II

The variation of the esterase isozyme, germination rate, chemical composition and digestibility of field bean(G1ycine soja S. and Z.) were estimated. The results are as follows; 1. The banding patterns of the esterase isozyme in field bean were varied wit

The esterase isozyme in tissue of wild legume plants were separated by horizontal starch gel electrophoresis. Extracts used in this study were prepared from fully expanded young leaf, cotyledon and radicle of seedling and root-nodule of Glycine sola, Vign

연어류의 종간교배 실험과 LDH, MDH, IDH, GODH, ME 등 다섯가지 isozyme에 대한 genetic marker로서의 활용 가능성을 알아보고자 1차적으로 연어, 산천어 및 무지개송어를 이용하여 종간교배를 실시하였고 이들 세종의 isozyme pattern을 비교하였다. 교배실험은 종간교배, 및 allotriploid 구간 등 12구간으로 나누어 실시하였으며 연어 암컷과 산천어 수컷의 교배결과가 초기성장 단계적에서 가장 우수하게 나타났고이

Starch gel electrophoresis was used to examine the banding pattern of Esterase isozyme in the leaf, root-nodule and seedling of four wild legume species, Trifolim repense, Glycine soja, Phaseolus nipponensis and Vigna uexillata. The number of band, enzyme

Red clover, ladino clover, white clover, alfalfa, 차풀 그리고 갈키나물등 6종의 콩과식물에서 잎과 줄기의 Esterase Isozyme를 추출하여 starch gel 전기영동법으로 분리한 후 염색하여 종간 차이점을 고찰하였다. 공시된 식물의 Esterase Isozyme의 band수, 염색강도, 이동속도는 종간에 차이가 있었다. 그러나 동일종에 있어서는 alfalfa를 제외하고는 잎과 줄기사이에 band의 수는 차

The soybean β-amylase [α-1, 4-glucan maltohydrolase, EC. 3. 2. 1. 2] is composed of seven isozymes( Ⅰ`, Ⅰ, Ⅱ, Ⅲ, Ⅳ, Ⅴ and Ⅵ), and isozyme Ⅱ and Ⅳ are the main components among these. The purification of β-amylase isozymes from soybean whey were performed by ammonium sulfate fractionation, CM-Sephadex C-50 column chromatography, DEAE-Sephadex chromatography and Gel filtration. The resulted purity of β-amylase was throughly confirmed by electrophoresis, and then determined its isoelectric point and molecular weight. The results obtained were as follows ; 1. Five active fractions of soybean β-amylase were derived on CM-Sephadex C-50 column chromatography . 2. Seven active bands of β-amylase isozymes were detected by isoelectric focusing gel electrophoresis, and their isoelectric points ( Ⅰ` to Ⅵ) were 5.07, 5.15, 5.25, 5.40, 5.55, 5.70 and 5.93, respectively. 3. Isozyme Ⅱ and Ⅳ were main components of soybean β-amylase. 4. The molecular weights of both isozyme Ⅱ and Ⅳ were determined to be 56, 000 daltons by the result of SDS polyacrylamide gel electrophoresis. 5. Km values of main isozyme Ⅱ & Ⅳ for amylopectin were determined to be 2.25㎎/㎖, which suggest the same function of each isozyme.