Purification and characterization of an exo .ALPHA.-1,2-mannanase from Flavobacterium dormitator var. glucanolyticae.
نویسندگان
چکیده
منابع مشابه
Purification and Characterization of Heparin Lyases from Flavobacterium heparinurn”
Heparin lyase I has been purified from Flavobacterium heparinum and has been partially characterized (Yang, V. C., Linhardt, R. J., Berstein, H., Cooney, C. L., and Langer, R. (1985) J. Biol. Chem. 260, 18491857). There has been no report of the purification of the other polysaccharide lyases from this organism. Although all three of these heparinlheparan sulfate lyases are widely used, with th...
متن کاملPURIFICATION AND PARTIAL CHARACTERIZATION O F PEROXIDASES FROM CULTIVATED RAPHANUS SATIVUS L. VAR. CICIL
Two peroxidases (EC. 1.11.1.7), POD I and POD II were purified from the roots of cultivatedRaphanus sativus L. Var. Cicil by one step ion-exchange chromatography after fractionation by acetone. The molecular weight of these enzymes were 43000 and 41000 Daltons and RZ 1.2 and 2.0 for POD I and POD II, respectively. Both enzymes consisted of a single polypeptide chain on SDS-PAGE. The maximum...
متن کاملPurification and Characterization of an Antibacterial, Antifungal and Non Hemolytic Peptide from Rana Ridibunda
Amphibians have a large variety of antimicrobial peptides that serve as natural innate barriers limiting microbial infection or, in some instances, act as an integral component in response to inflammation or microbial infection. A novel peptide with antibacterial effects and without hemolytic activity was purified from skin secretions of Rana ridibunda by multisteps cation-exchange FPLC, revers...
متن کاملIsolation, Purification and Characterization of Mannanase from Bacillus subtilis MAN-511
A bacterium, MAN-511 that produced extracellular mannanase, was isolated and identified as Bacillus subtilis on the basis of 16S rDNA phylogenetic analysis. The enzyme was purified to apparent homogeneity by precipitasi ammonium sulfat 70% and Sephadex G-75 chromatography procedures. The mannanase was purified 7.6 fold and specificity of 9.3 U/mg protein. SDS-PAGE of the purified enzyme showed ...
متن کاملPurification and partial characterization of an agglutinin from Phaseolus coccineus var. 'alubia'.
An agglutination from seeds of 'alubia', a Mexican strain of Phaseolus coccineus, has been purified by affinity chromatography using physically entrapped stroma. The protein appears to be homogeneous by electrophoresis, molecular sieve chromatography and ultracentrifugation. A molecular species of approx. Mr 112,000, with S values of 6.25, 4.52, 4.63 and 4.65 at pH 2.5, 4.5, 7.0 and 9.5, respec...
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: 1975
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.39.1981