Purification and properties of clostridiopeptidase B (Clostripain).
نویسندگان
چکیده
The proteolytic enzyme, clostridiopeptidase B (clostripain), from Clostridium histo2yticum culture filtrates has been purified to apparent homogeneity as judged by ultracentrifugation, electrophoresis in polyacrylamide gels, immunodiffusion, and immunoelectrophoresis. The enzyme has an apparent molecular weight of 50,000 from sedimentation equilibrium studies. Optical rotatory dispersion studies suggest a low a-helical content. Clostridiopeptidase B exhibits proteolytic as well as amidase-esterase properties. The specificity is confined primarily to arginine residues, although hydrolysis proceeds to a minor degree in most lysine-containing substrates.
منابع مشابه
Clostripain, the Missing Link in the Enzyme Blend for Efficient Human Islet Isolation
UNLABELLED Effective digestive enzymes are crucial for successful islet isolation. Supplemental proteases are essential as they synergize with collagenase for effective pancreas digestion. The presence of tryptic-like activity has been implicated in efficient enzyme blends and the present study aimed to evaluate if addition of clostripain, an enzyme with tryptic-like activity, could improve eff...
متن کاملPURIFICATION AND PROPERTIES OF RAT GASTROCNEMIUS MUSCLE N-ACETYL-I3-DGLUCOSAMINIDASE A AND B.
N-acetyl-B-D-Glucosaminidase was purified by affinity and ionexchange chromatography. Two major, A and B, and three minor intermediate forms were isolated and characterized. NAG-A and NAG-B were purified 440 and 1200 fold with final yields of 16 and 23 percent respectively. Each activity was represented by a single protein band. After 70 min preincubation at 55°C a loss of70% activity of N...
متن کاملSynthesis of lysine-containing sulphonium salts and their properties as proteinase inhibitors.
Some sulphonium salts derived from lysine were synthesized with the general structure R-Lys-CH2S+-(alkyl)2. They were examined as inhibitors of the cysteine proteinase clostripain, which has a preference for cleaving peptide bonds at the carboxy group of basic amino acids, and of a number of trypsin-related serine proteinases. Clostripain was irreversibly inactivated by all reagents examined, b...
متن کاملPurification and biochemical properties of a thermostable, haloalkaline cellulase from Bacillus licheniformis AMF-07 and its application for hydrolysis of different cellulosic substrates to bioethanol production
A thermophilic strain AMF-07, hydrolyzing carboxymethylcellulose (CMC) was isolated from Kerman hot spring and was identified as Bacillus licheniformis based on 16S rRNA sequence homology. The carboxymethylcellulase (CMCase) enzyme produced by the B. licheniformis was purified by (NH4)2SO4 precipitation, ion exchange and gel filtration chromatography. The purified enzyme gave a single band on S...
متن کاملInteractions of tervalent lanthanide ions with bacterial collagenase (clostridiopeptidase A).
Tervalent cations of the lanthanide (rare-earth) elements reversibly inhibit bacterial collagenase (clostridiopeptidase A; EC 3.4.24.3). Sm(3+), whose ionic radius is closest to that of Ca(2+), is the most effective inhibitor, completely suppressing clostridiopeptidase activity at a concentration of 100mum in the presence of 5mm-Ca(2+). Er(3+) and Lu(3+), which both have ionic radii smaller tha...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 243 18 شماره
صفحات -
تاریخ انتشار 1968