Glycosylation of Protein by Conjugation of Periodate-Oxidized Sugars

과요오드산 산화당에 의한 인공 당단백질의 조제

Periodate-oxidized soluble starch and maltohexaose, maltotetraose, maltose, and glyceraldehyde reacted with sweet potato ${\beta}-amylase$, wheat ${\beta}-amylase$, aldolase, bovine serum albumin, catalase, carboxypeptidase, ferritin and pronase. Electrophoretical mobility of modified proteins was different from that of native proteins, and modified proteins were stained with periodic acid-Schiff while native proteins did not stain. This results means that oxidized sugars attached on proteins. This bond is based on the Schiffs base between CHO group of oxidized sugar and ${\varepsilon}-NH_2$ group of lysine of protein. There is no changed UV absorption spectrum of sweet potato ${\beta}-amylase$ modified with oxidized soluble starch, in comparison with native enzyme.

과요오드산 산화 가용성전분 및 말토올리고당을 고구마 ${\beta}-amylase$, 밀 ${\beta}-amylase$, aldolase, bovine serum albumin, catalase, carboxypeptidase, ferritin, pronase와 반응시켜서 전기영동하였다. 이들 단백질은 전기영동상의 이동도가 달라지고, 단백질 밴드와 같은 위치에서 PAS 염색 밴드를 나타내어 당이 부가된 것으로 확인되었다. 당의 부가는 과요오드산 산화당의 알데히드기가 단백질 분자 표면 리신의 ${\varepsilon}-NH_2$기와 Schiff 염기를 형성하여 일어난다. 변형효소는 자외흡광곡선에 변화를 나타내지 않았다.