Granum P E, Nissen H
Department of Food Hygiene, Norwegian College of Veterinary Medicine, Oslo.
FEMS Microbiol Lett. 1993 Jun 1;110(1):97-100. doi: 10.1111/j.1574-6968.1993.tb06301.x.
The three components of the 'enterotoxin complex' have been purified and the sequence of the first 14-15 amino acids of the proteins determined. Limited homology was found in the N-terminal sequence of the three proteins. The molecular mass of the proteins was determined to be 48, 40 and 34 kDa, respectively. Only the 40-kDa protein was toxic to Vero cells, whilst the 34-kDa protein was found to be hemolytic. The sequence of the first 14 N-terminal amino acids of this protein was identical to the sequence of the sphingomyelinase residues 28-41 (the N-terminal after loss of the signal sequence), except for a change from Gln to Glu in position 33 of the sphingomyelinase sequence.
“肠毒素复合物”的三个组分已被纯化，并且已确定了这些蛋白质前14 - 15个氨基酸的序列。在这三种蛋白质的N端序列中发现了有限的同源性。这些蛋白质的分子量分别测定为48、40和34 kDa。只有40 kDa的蛋白质对Vero细胞有毒性，而34 kDa的蛋白质被发现具有溶血作用。该蛋白质前14个N端氨基酸的序列与鞘磷脂酶残基28 - 41的序列（信号序列缺失后的N端）相同，只是鞘磷脂酶序列第33位的谷氨酰胺变为谷氨酸。
