STUDIES ON NEW ACID PROTEASES FROM SCYTALIDIUM-LIGNICOLUM M-133 .2. PURIFICATION AND SOME ENZYMATIC PROPERTIES OF ACID PROTEASE A AND B OF SCYTALIDIUM-LIGNICOLUM ATCC 24568
STUDIES ON NEW ACID PROTEASES FROM SCYTALIDIUM-LIGNICOLUM M-133 .2. PURIFICATION AND SOME ENZYMATIC PROPERTIES OF ACID PROTEASE A AND B OF SCYTALIDIUM-LIGNICOLUM ATCC 24568
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DOI：
10.1080/00021369.1974.10861522
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发表时间：
1974-01-01
期刊：
影响因子：
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通讯作者：
MURAO, S
中科院分区：
文献类型：
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作者：
ODA, K;MURAO, S
从Scytalidium lignicolumATCC 24568的培养滤液中纯化出3种酸性蛋白酶。从1升培养液中获得约3mg的A-1、6mg的A-2和60mg的B。根据超速离心分析和圆盘电泳等物理化学标准，这些纯化的酶是单分散的。除了等电点差异较小之外，A-1 和 A-2 的酶学性质非常相似。 A-1 和 A-2 在 pH 3.0~3.5 范围内对酪蛋白具有活性，并在 37°C 下在 pH 2.5 至 5.5 范围内稳定 20 小时。两种酶均被NBS强烈抑制，但被EDTA、DFP和巯基试剂抑制。B在pH 2.0时最活跃，并且在pH值1.5和5.0之间稳定。该酶也被NBS和KMnO4抑制，但被EDTA、DFP和巯基试剂抑制。A-1、A-2和B的分子量和等电点均为43,000，pH 3.6；分别为 43,000，pH 3.8 和 22,000，pH 3.2。A-1 和 A-2 不受 S-PI 和合成胃蛋白酶抑制剂（如重氮乙酰基-dl-正亮氨酸甲酯 (DAN) 和 1,2-环氧-3-(对硝基苯氧基)-丙烷 (EPNP)）的抑制。 B 被 EPNP 抑制，但不被 S-PI 和 DAN 抑制。
Three kinds of acid proteases were purified from the culture filtrate ofScytalidium lignicolumATCC 24568. About 3 mg of A–1, 6 mg of A–2 and 60 mg of B were obtained from one liter of culture broth. These purified enzymes were monodisperse by physicochemical criteria such as ultracentrifugal analysis and disc electrophoresis.A–1 and A–2 were very similar to each other on their enzymatic properties except the small difference of isoelectric point. A–1 and A–2 were active between pH 3.0~3.5 toward casein, and stable between pH 2.5 and 5.5 for 20 hr at 37°C. Both enzymes were strongly inhibited by NBS, but not by EDTA, DFP and sulfhydryl reagents.B was most active at pH 2.0, and stable at pH values between 1.5 and 5.0. This enzyme was also inhibited by NBS and KMnO4, but not by EDTA, DFP and sulfhydryl reagents.The molecular weights and isoelectric points of A–1, A–2 and B were 43,000, pH 3.6; 43,000, pH 3.8 and 22,000, pH 3.2, respectively.A–1 and A–2 were not inhibited by S–PI and synthetic pepsin inhibitor such as diazoacetyl-dl-norleucine methylester (DAN) and 1,2-epoxy-3-(p-nitrophenoxy)-propane (EPNP). B was inhibited by EPNP, but not by S–PI and DAN.