소나무 화분으로 부터 branched-chain 아미노산 아미노기 전위 효소 [EC 2. 6. 1. 6]를 검출하기 위하여 화분의 마쇄액을 분별 원심분획한 결과 전체 효소 활성도의 86%가 세포질 분획에서 측정되었고 상기 효소를 정제하기 위하여 DEAE-cellulose column chromatogaphy를 행한 결과 유출용 인산엽 완충액의 농도 180 및 200mM에서 효소 II와 III이 각각 검출되었다. 상기 소나무 화분의 효소 II와 III은 정상 백서의 간 및 뇌 조직에서 추출 정제된 효소와 같은 농도의 유출용 완충액에서 검출된 점으로 미루어 상기 효소들의 성상이 같은 것으로 생각되며 소나무 화분의 경우 효소 II의 비활성도는 III에 비하여 약 2.5배의 활성도를 보였고 이 효소 II 및 III은 chromatography 결과 각각 150배 및 125배로 정제되었다
A study was undertaken on the distribution of branched-chain amino acid aminotransferase (EC 2. 6. 1. 6.) in pine pollen. About 86% of the total enzyme activity was recovered in cytosol fraction, and further purification was carried out with DEAE-cellulose column chromatography. It was demonstrated that there were two types of isozymes in pollen cytosol fraction such as Enzyme II and Enzyme III. One enzyme (enzyme II) was eluted by 180mM phosphate buffer from a DEAE-cellulose column and was specific for leucine. The other enzyme (enzyme III) was eluted by 200mM phosphate buffer and catalyzed the transamination of all three amino acids. The chromatographic elution profile of the enzymes II and III from the pine pollen was very similar with those of normal rat liver and brain. It was found that the enzyme activity was higher in enzyme II than enzyme III. The enzyme II and III were purified about 150 and 125-folds increases in specific activities after chromatography on DEAE-cellulose. The properties of these enzymes are currently under investigation.
