Skrypal' I H, Baichev V V, Karanda T M
Mikrobiol Z. 1996 Jan-Feb;58(1):15-22.
Four strains of mollicutes different in their role in pathology of people, animals and plants have been studied to detect general proteolytic (caseinolytic) activity with results presented. Proteolytic activity was determined both in the deposited proteins and in supersediment liquids under suturation with ammonium sulphate of 55 and 80%, respectively. Maximum proteolytic activity was observed in supersediment liquids. It was 137.2 E per 1 mg of protein in M. fermentans PG-18; 106.2 in A. laidlawii PG-8; 61.8 in A. laidlawii var. granulum 118 and 11.5 E per 1 mg of protein in M. pneumoniae FH. In the sediments of studied mollicutes proteolytic (caseinolytic) activity was also found but it was considerably less. The relation of proteolytic enzymes found in the sediment being quantitatively expressed, the following proportion will be obtained: 118:FH:PG-18:PG-8=8.8:2.3:2.8:1. Sediments can serve initial material for isolation of these enzymes and for detailed study of their properties.
对在人类、动物和植物病理学中作用不同的四株支原体进行了研究,以检测其总体蛋白水解(酪蛋白水解)活性,并给出了结果。分别在55%和80%硫酸铵饱和度下,对沉淀蛋白和上清液中的蛋白水解活性进行了测定。在上清液中观察到最大蛋白水解活性。在发酵支原体PG-18中,每1毫克蛋白质的蛋白水解活性为137.2 E;在莱氏无胆甾原体PG-8中为106.2;在莱氏无胆甾原体颗粒变种118中为61.8;在肺炎支原体FH中为每1毫克蛋白质11.5 E。在所研究的支原体沉淀物中也发现了蛋白水解(酪蛋白水解)活性,但活性要低得多。沉淀物中发现的蛋白水解酶的关系以定量表示,将得到以下比例:118:FH:PG-18:PG-8 = 8.8:2.3:2.8:1。沉淀物可作为分离这些酶及其性质详细研究的起始材料。