Zamotrinskiĭ A V, Malyshev I Iu, Meerson F Z
Biull Eksp Biol Med. 1992 Jun;113(6):586-7.
The hsp 70 content was measured in the myocardium of a control rat group, in the group of rats 24 hours following a heat shock and in the group of rats 48 hours after a heat shock. In 24 hours after the heat shock, a major inducible hsp 70 with molecular weight of 71 kDa and pI about 5.8 occurred which was utterly absent in myocardial cytosol from control animals. In addition, there was an increase in polypeptide fraction with molecular weight of 73 kDa and pI about 5.6 (HSX73). In 48 hours after the heat shock, first the inducible hsp 70 with molecular weight of 71 kDa and pI about 5.8 disappeared which was found in 24 hours; secondly, HSX73 decreased to the control level and, thirdly, several isoforms pronouncedly accumulated with molecular weight of about 71 kDa and pI ranging from 5.9 to 6.3. Thus, the isoform composition of stress proteins induced by heat shock strongly depends on the time after the stress exposure. Furthermore, the accumulation of more acidic isoforms precedes the accumulation of alkaline ones.
在对照大鼠组、热休克后24小时的大鼠组以及热休克后48小时的大鼠组的心肌中测量hsp 70含量。热休克后24小时,出现了一种主要的诱导型hsp 70,其分子量为71 kDa,pI约为5.8,而对照动物的心肌细胞质中完全没有这种蛋白。此外,分子量为73 kDa、pI约为5.6的多肽组分(HSX73)有所增加。热休克后48小时,首先,24小时时发现的分子量为71 kDa、pI约为5.8的诱导型hsp 70消失;其次,HSX73降至对照水平;第三,几种异构体明显积累,分子量约为71 kDa,pI范围为5.9至6.3。因此,热休克诱导的应激蛋白的异构体组成强烈依赖于应激暴露后的时间。此外,酸性更强的异构体的积累先于碱性异构体的积累。