Hashizume T, Park W, Matsuhashi M
J Antibiot (Tokyo). 1984 Sep;37(9):1049-53. doi: 10.7164/antibiotics.37.1049.
Penicillin-binding proteins 1, 2 and 3 in Staphylococcus aureus were found to possess common properties. All have very strong affinities for both benzylpenicillin and imipenem (N-formimidoylthienamycin), and all have an activity which releases bound imipenem, but not bound benzylpenicillin. Lower molecular weight penicillin-binding protein 4, which has a rather weak affinity for benzylpenicillin and also weak penicillinase activity showed an extraordinarily high affinity for imipenem but no antibiotic-releasing activity.
金黄色葡萄球菌中的青霉素结合蛋白1、2和3具有共同特性。它们对苄青霉素和亚胺培南（N-甲酰亚胺硫霉素）都有很强的亲和力，并且都具有一种能释放结合的亚胺培南但不能释放结合的苄青霉素的活性。分子量较低的青霉素结合蛋白4对苄青霉素的亲和力较弱，且青霉素酶活性也较弱，但它对亚胺培南表现出极高的亲和力，且没有抗生素释放活性。
