Schalinatus E, Ruttloff H, Behnke U
Nahrung. 1983;27(4):379-86. doi: 10.1002/food.19830270410.
The intracellular proteases (IP) of the cellular extract of Thermoactinomyces vulgaris are characterized as to the biochemical properties compared with the corresponding extracellular proteases (EP). According to that, the storage stability and the temperature and pH behaviour (optimum, stability) of both of the proteases are identical. Nevertheless, differences were detected between IP and EP after the action of several effectors and different substrates. As could be seen after a column chromatographic separation of the IP of the cellular extract, it is composed of at least 3 proteases, two of them are serine proteases which can be inhibited moreover unspecifically by p-chloromercuri benzoate. The purified proteases (IP) are very instable and therefore not yet characterized in detail.
将普通嗜热放线菌细胞提取物中的细胞内蛋白酶（IP）与相应的细胞外蛋白酶（EP）的生化特性进行了比较。据此，两种蛋白酶的储存稳定性以及温度和pH行为（最适值、稳定性）是相同的。然而，在几种效应物和不同底物作用后，检测到IP和EP之间存在差异。从细胞提取物的IP经柱色谱分离后可以看出，它至少由3种蛋白酶组成，其中两种是丝氨酸蛋白酶，此外还可被对氯汞苯甲酸非特异性抑制。纯化后的蛋白酶（IP）非常不稳定，因此尚未进行详细表征。
