Adinolfi A, Leone N, Swallow D, Hopkinson D A, Zapponi M C, Ferri G, Camardella L, Ronchi S
International Institute of Genetics and Biophysics, CNR, Naples, Italy.
Exp Clin Immunogenet. 1991;8(2):96-106.
Two monoclonal antibodies raised against native horse alcohol dehydrogenase (HADH) bind preferentially to the enzyme attached to solid supports and recognize the denatured and carboxymethylated HADH subunits. Both antibodies cross-react with the human class I isoenzymes but do not recognize the class III ADH isoenzyme. Protease digestion, electrophoresis and HPLC have been used to identify the linear epitope which is contained in the sequence Pro344-Glu357 of the HADH subunit.
两种针对天然马醇脱氢酶(HADH)产生的单克隆抗体优先结合附着在固相支持物上的该酶,并识别变性和羧甲基化的HADH亚基。两种抗体都与人I类同工酶发生交叉反应,但不识别III类ADH同工酶。蛋白酶消化、电泳和高效液相色谱已被用于鉴定HADH亚基序列Pro344-Glu357中包含的线性表位。