Trop M, Birk Y
Biochem J. 1970 Jan;116(1):19-25. doi: 10.1042/bj1160019.
Purification of pronase by ion-exchange chromatography gave four proteolytically active fractions. Fraction A(2) contained an endopeptidase that attacks poly l-valine. Fraction B contained an endopeptidase, an aminopeptidase and carboxypeptidases. The activities against hippuryl-l-arginine and hippuryl-l-phenylalanine could be inhibited to a considerable extent by di-isopropyl phosphorofluoridate and by EDTA. Fraction C contained an endopeptidase resembling bovine trypsin. The pure enzyme was completely inactivated by di-isopropyl phosphorofluoridate and pancreatic trypsin inhibitor and to about 90% by other naturally occurring trypsin inhibitors. Fraction D contained an apparently homogeneous endopeptidase, inhibited by diisopropyl phosphorofluoridate, that adsorbed to and hydrolysed elastin. The activity of all these fractions was tested qualitatively against a wide range of small peptides and synthetic substrates.
通过离子交换色谱法纯化链霉蛋白酶得到了四个具有蛋白水解活性的组分。组分A(2)含有一种攻击聚L-缬氨酸的内肽酶。组分B含有一种内肽酶、一种氨肽酶和羧肽酶。对马尿酰-L-精氨酸和马尿酰-L-苯丙氨酸的活性可被二异丙基氟磷酸酯和EDTA相当程度地抑制。组分C含有一种类似于牛胰蛋白酶的内肽酶。纯酶被二异丙基氟磷酸酯和胰蛋白酶抑制剂完全灭活，被其他天然存在的胰蛋白酶抑制剂灭活约90%。组分D含有一种明显均一的内肽酶，被二异丙基氟磷酸酯抑制，该内肽酶能吸附并水解弹性蛋白。针对多种小肽和合成底物对所有这些组分的活性进行了定性测试。
