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Normal human serum was found to inhibit human cathepsin B1. 2. The major inhibitor present in serum was purified and identified as alpha(2)-macroglobulin. 3. alpha(2)-Macroglobulin was found to bind cathepsin B1 in an approximately 1:1 molar ratio. When bound, the enzyme retained about 50% of its proteolytic activity, and up to 80% of its activity against alpha-N-benzoyl-dl-arginine 2-naphthylamide. 4. Pretreatment of alpha(2)-macroglobulin with cathepsin B1 inactivated by exposure to pH8.5 or iodoacetic acid, in large molar excess, did not prevent the subsequent binding of active enzyme. Active enzyme, once bound, was not protected from inhibition by 1-chloro-4-phenyl-3-tosylamido-l-butan-2-one. 5. Cathepsin B1 was also inhibited by human immunoglobulin G, at high concentration. 6. Because it had been suggested that haptoglobin is responsible for the inhibition of ;cathepsin B' by serum, a method was devised for the selective removal of haptoglobin from mixtures of serum proteins by adsorption on haemoglobin covalently linked to Sepharose. No evidence was obtained that haptoglobin has any inhibitory activity against the enzyme.

发现正常人血清可抑制人组织蛋白酶B1。
血清中存在的主要抑制剂被纯化并鉴定为α(2)-巨球蛋白。
发现α(2)-巨球蛋白以大约1:1的摩尔比结合组织蛋白酶B1。结合后，该酶保留了约50%的蛋白水解活性，以及高达80%的针对α-N-苯甲酰-dl-精氨酸2-萘酰胺的活性。
用暴露于pH8.5或碘乙酸而失活的组织蛋白酶B1对α(2)-巨球蛋白进行预处理，即使摩尔过量很大，也不能阻止随后活性酶的结合。活性酶一旦结合，就不能免受1-氯-4-苯基-3-甲苯磺酰胺基-1-丁酮-2-酮的抑制。
人免疫球蛋白G在高浓度时也能抑制组织蛋白酶B1。
因为有人提出触珠蛋白负责血清对“组织蛋白酶B”的抑制作用，所以设计了一种方法，通过吸附在与琼脂糖共价连接的血红蛋白上来从血清蛋白混合物中选择性去除触珠蛋白。没有证据表明触珠蛋白对该酶有任何抑制活性。

Normal human serum was found to inhibit human cathepsin B1. 2. The major inhibitor present in serum was purified and identified as alpha(2)-macroglobulin. 3. alpha(2)-Macroglobulin was found to bind cathepsin B1 in an approximately 1:1 molar ratio. When bound, the enzyme retained about 50% of its proteolytic activity, and up to 80% of its activity against alpha-N-benzoyl-dl-arginine 2-naphthylamide. 4. Pretreatment of alpha(2)-macroglobulin with cathepsin B1 inactivated by exposure to pH8.5 or iodoacetic acid, in large molar excess, did not prevent the subsequent binding of active enzyme. Active enzyme, once bound, was not protected from inhibition by 1-chloro-4-phenyl-3-tosylamido-l-butan-2-one. 5. Cathepsin B1 was also inhibited by human immunoglobulin G, at high concentration. 6. Because it had been suggested that haptoglobin is responsible for the inhibition of ;cathepsin B' by serum, a method was devised for the selective removal of haptoglobin from mixtures of serum proteins by adsorption on haemoglobin covalently linked to Sepharose. No evidence was obtained that haptoglobin has any inhibitory activity against the enzyme.

发现正常人血清可抑制人组织蛋白酶B1。
血清中存在的主要抑制剂被纯化并鉴定为α(2)-巨球蛋白。
发现α(2)-巨球蛋白以大约1:1的摩尔比结合组织蛋白酶B1。结合后，该酶保留了约50%的蛋白水解活性，以及高达80%的针对α-N-苯甲酰-dl-精氨酸2-萘酰胺的活性。
用暴露于pH8.5或碘乙酸而失活的组织蛋白酶B1对α(2)-巨球蛋白进行预处理，即使摩尔过量很大，也不能阻止随后活性酶的结合。活性酶一旦结合，就不能免受1-氯-4-苯基-3-甲苯磺酰胺基-1-丁酮-2-酮的抑制。
人免疫球蛋白G在高浓度时也能抑制组织蛋白酶B1。
因为有人提出触珠蛋白负责血清对“组织蛋白酶B”的抑制作用，所以设计了一种方法，通过吸附在与琼脂糖共价连接的血红蛋白上来从血清蛋白混合物中选择性去除触珠蛋白。没有证据表明触珠蛋白对该酶有任何抑制活性。

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