Traficante L J, Lampen J O
Biochim Biophys Acta. 1977 May 16;467(1):44-50. doi: 10.1016/0005-2736(77)90240-1.
A substantial fraction of the total membrane penicillinase of Bacillus licheniformis 749/C is attached to the vesicles released during conversion of the cells to protoplasts. This enzyme was purified since there was indirect evidence that it differed from the enzyme that remained with the protoplast. The purified vesicle penicillinase has the same molecular weight and general properties as the plasma membrane (protoplast) enzyme and, similarly, contains a covalently linked phosphatidylserine residue. Treatment of the two enzymes with trypsin produced phosphatidylserine-containing peptides which could not be distinguished by gel or paper electrophoresis. The two membrane penicillinases are very similar, if not identical.
地衣芽孢杆菌749/C的总膜青霉素酶中有很大一部分附着在细胞转化为原生质体过程中释放的囊泡上。由于有间接证据表明这种酶与留在原生质体中的酶不同，因此对其进行了纯化。纯化后的囊泡青霉素酶与质膜（原生质体）酶具有相同的分子量和一般性质，同样含有一个共价连接的磷脂酰丝氨酸残基。用胰蛋白酶处理这两种酶会产生含磷脂酰丝氨酸的肽，通过凝胶或纸电泳无法区分。这两种膜青霉素酶即使不完全相同，也非常相似。
