Enzymatic Properties of Dipeptidyl Carboxypeptidase from Bacillus Pumilus.
نویسندگان
چکیده
منابع مشابه
Enzymatic properties of dipeptidyl carboxypeptidase from Bacillus pumilus.
Enzymatic properties of dipeptidyl carboxypeptidase (DCP) from Bacillus pumilus were investigated. The enzyme was more active on tri- and tetrapeptides than angiotensin-converting enzyme (ACE) from rabbit lung. The presence of chloride ion is essential for the hydrolysis. The Km value of angiotensin I for the enzyme was 0.119 x 10(-3) M. The enzyme was not inhibited by the mammalian ACE inhibit...
متن کاملLipase from Bacillus pumilus RK31: Production, Purification and Some Properties
A new lipolytic strain of Bacillus sp. was isolated from oil contaminated soil sample. On measurement of biochemical parameters and 16S rDNA sequence information the strain was identified as Bacillus pumilus RK31 (NCBI accession no GQ463238). The lipase purification steps involved, 60% ammonium sulphate saturation, gel filtration chromatography using Sephadex G200 and ion exchange chromatograph...
متن کاملSome properties of the PBP1 transduction system in Bacillus pumilus.
Bacteriophage PBP1 is a flagella-specific virus that performs generalized transduction in strains of Bacillus pumilus. PBP1 is morphologically and serologically distinct from two other flagella-specific phages, PBS1 and SP-15, which perform generalized transduction in certain Bacillus species. The DNA extracted from PBP1 particles has a buoyant density of 1.690 g/cm(3) in cesium chloride gradie...
متن کاملDipeptidyl carboxypeptidase-deficient mutants of Salmonella typhimurium.
Mutants of Salmonella typhimurium deficient in dipeptidyl carboxypeptidase have been isolated by screening for clones unable to use N-acetyl-L-alanyl-L-alanyl-L-alanine (AcAla3) as the sole nitrogen source. An insertion of the transposable element Tn10 near dcp (the locus coding for dipeptidyl carboxypeptidase) has been isolated and used to map the locus in the interval between purB and trp, an...
متن کاملD=Alanine Carboxypeptidase from Bacillus subtilis Membranes
The D-alanine carboxypeptidase was solubilized from the membranes of Bacillus subtilis with the nonionic detergent, Triton X-100, and pursed to homogeneity. The purified protein bound irreversibly radioactivity from [Wlpenicillin G. It contained a single polypeptide chain of molecular weight 50,000 and existed in solution as a protein-detergent aggregate of molecular weight about 350,000. The a...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1991
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.55.1695