Storm D R, Blumberg P M, Strominger J L
J Bacteriol. 1974 Feb;117(2):783-5. doi: 10.1128/jb.117.2.783-785.1974.
An insoluble penicillin derivative, 6-aminopenicillanic acid covalently coupled to Sepharose, was used to investigate the location of the d-alanine carboxypeptidase in the Bacillus subtilis membrane. Only 50% of the enzymatic activity in protoplasts and 74% of that in purified membranes was sensitive, although the purified enzyme could be inhibited completely by the resin. These results suggest that a minimum of 50% of the d-alanine carboxypeptidase exists on the outer face of the bacterial membrane.
一种不溶性青霉素衍生物，即与琼脂糖共价偶联的6-氨基青霉烷酸，被用于研究枯草芽孢杆菌膜中d-丙氨酸羧肽酶的定位。尽管纯化的酶可被该树脂完全抑制，但原生质体中只有50%的酶活性以及纯化膜中74%的酶活性是敏感的。这些结果表明，至少50%的d-丙氨酸羧肽酶存在于细菌膜的外表面。
