Emöd I, Tong N T, Keil B
Biochim Biophys Acta. 1981 Jun 15;659(2):283-91. doi: 10.1016/0005-2744(81)90054-1.
Pure collagenase (clostridiopeptidase A, EC 3.4.24.3) having a molecular weight of 70 000 was obtained from the culture medium of Clostridium histolyticym by a combination of ultrafiltrations, molecular sieve, affinity and hydrophobic chromatography. The value of its specific activity is the highest of those described previously but 6-times lower than that of the collagenase from Achromobacter iophagus (EC 3.4.24.8). Its amino acid composition differs from previous data, namely by the presence of cysteine, methionine, tryptophan and O-phosphoserine residues. In contrast to Achromobacter collagenase it does not dissociate in subunits during the deactivation by EDTA or LiCl/glycine buffer at pH 10.5. Existence of multiple forms of Clostridium collagenase previously described is discussed as being due to autolysis of a single molecular species or to a different degree of phosphorylation.
通过超滤、分子筛、亲和色谱和疏水色谱相结合的方法，从溶组织梭菌的培养基中获得了分子量为70000的纯胶原酶（梭菌肽酶A，EC 3.4.24.3）。其比活性值是先前报道中最高的，但比食油无色杆菌胶原酶（EC 3.4.24.8）低6倍。其氨基酸组成与先前数据不同，即存在半胱氨酸、蛋氨酸、色氨酸和O-磷酸丝氨酸残基。与食油无色杆菌胶原酶不同，在pH 10.5的EDTA或LiCl/甘氨酸缓冲液失活过程中，它不会解离成亚基。先前描述的梭菌胶原酶多种形式的存在被认为是由于单一分子物种的自溶或不同程度的磷酸化。
