Lund T, Granum P E
Department of Pharmacology, Microbiology and Food Hygiene, Norwegian School of Veterinary Science, Oslo, Norway.
FEMS Microbiol Lett. 1999 Sep 15;178(2):355-61. doi: 10.1111/j.1574-6968.1999.tb08699.x.
A sequence of 91 amino acids residues, probably starting from the N-terminal of the mature protein, was determined for the 105-kDa protein of the non-haemolytic enterotoxin of Bacillus cereus. The last part of this sequence was similar to parts of the N-terminal portions of two collagenases of Clostridium histolyticum and Clostridium perfringens. Zymography, with intact collagen fibril and gelatin as substrates, showed that the 105-kDa protein had collagenolytic and gelatinolytic activity. The 105-kDa protein also showed activity against a typical collagenase substrate, azocoll, and was inhibited by EDTA and 1,10-phenanthroline. We conclude that the 105-kDa protein is a collagenase.
已确定蜡样芽孢杆菌非溶血型肠毒素105 kDa蛋白的91个氨基酸残基序列，该序列可能从成熟蛋白的N端开始。此序列的最后部分与溶组织梭菌和产气荚膜梭菌两种胶原酶N端部分的序列相似。以完整胶原纤维和明胶为底物的酶谱分析表明，105 kDa蛋白具有胶原分解和明胶分解活性。该105 kDa蛋白对典型的胶原酶底物偶氮胶原也有活性，并受到EDTA和1,10-菲咯啉的抑制。我们得出结论，105 kDa蛋白是一种胶原酶。
